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50S ribosomal subunit assembly factor
UniProt
archaeal initiation factor 2
archaeal initiation factor 2C
-
-
archaeal translation initiation factor 2
-
BPI-inducible protein A
-
chloroplast elongation factor G
-
-
eEF1A
genes A1, A2, A3, A4
elongation factor (EF)
-
-
-
elongation factor 1 alpha
elongation factor thermo unstable
-
elongation factor-1alpha
-
elongation factor-1beta
-
elongation factor-like 1 GTPase
eukaryotic elongation factor 2
-
eukaryotic elongation factor one alpha
-
eukaryotic initiation factor 2
-
-
eukaryotic initiation factor 2A
-
-
eukaryotic initiation factor 5B
-
-
eukaryotic translation initiation factor 2
eukaryotic translation initiation factor 5B
-
GTP phosphohydrolase
-
-
-
GTPase-activating protein
-
-
guanine triphosphatase
-
-
-
guanine-nucleotide-exchange factor of eIF2
-
guanosine 5'-triphosphatase
-
-
-
initiation factor (IF)
-
-
-
initiation factor aIF5B
-
-
mitochondrial elongation factor G
-
-
mitochondrial initiation factor 2
-
-
peptide-release or termination factor
-
-
-
protein-synthesizing GTPase
-
-
protein-sythesizing GTPase
ribosome-bound initiation factor 2
-
ribosome-dependent GTPase
selenocysteine tRNA-specific elongation factor
-
-
signal recognition particle GTPase Ffh
-
-
translation elongation factor 2
-
translation factor aIF2/5B
-
-
translation initiation factor
-
translation initiation factor 2
translation initiation factor 2 gamma
translation initiation factor 5B
translation initiation factor eIF5
-
-
translation initiation factor IF1
-
-
translation initiation factor IF2
translation termination factor eRF3
-
-
translational guanosine triphosphatase
-
translational initiation factor 2
-
-
aEF-1alpha

-
-
aIF2

-
-
aIF2-gamma

-
aIF5B

-
-
archaeal initiation factor 2

-
-
archaeal initiation factor 2
-
EF-1alpha

-
-
EF-G

-
-
EF-like GTPase

-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
Pleodorina sp.
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-like GTPase
-
a class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha
EF-Tu

-
-
EF4

-
-
EFL

-
-
Efl1

-
Efl1 GTPase

-
eIF2

-
eIF5B

-
elongation factor 1 alpha

-
-
elongation factor 1 alpha
-
-
elongation factor 1alpha

-
-
657934, 658537, 667607, 678126, 678196, 679625, 679722, 691101, 724487, 724710, 724936
elongation factor 1alpha
-
elongation factor 4

-
-
elongation factor G

-
-
elongation factor Tu

-
-
elongation factor-like 1

-
elongation factor-like 1
-
elongation factor-like 1
-
elongation factor-like 1 GTPase

-
elongation factor-like 1 GTPase
-
elongation factor-like 1 GTPase
-
eukaryotic translation initiation factor 2

-
eukaryotic translation initiation factor 2
-
-
GTPase

-
-
-
GTPase HflX

-
-
guanosine triphosphatase

-
-
-
guanosine triphosphatase
-
HflX GTPase

-
IF2

-
-
IF2 GTPase

-
-
IF3

-
-
infB

-
-
initiation factor 2

-
-
initiation factor 3

-
-
initiation factor 5B

-
-
L11

-
-
LepA

-
-
protein-sythesizing GTPase

-
-
protein-sythesizing GTPase
-
ribosome-dependent GTPase

-
ribosome-dependent GTPase
-
-
ribosome-dependent GTPase
-
-
ribosome-dependent GTPase
-
-
Ss-aIF2

-
SsEF-1alpha

-
-
SsEF-1alpha
amino acid at position 15, strain MT3 valine, SsMT3EF-1alpha, strain MT4 isoleucine, SsMT4EF-1alpha
SsGBP

-
SSO0269

locus name
SSO0412

locus name, gamma-subunit
SSO0412
locus name, gamma-subunit
SSO1050

locus name, alpha-subunit
SSO1050
locus name, alpha-subunit
SSO2381

locus name, beta-subunit
SSO2381
locus name, beta-subunit
SsoHflX

-
translation initiation factor 2

-
translation initiation factor 2
-
-
translation initiation factor 2
-
-
translation initiation factor 2
-
translation initiation factor 2
-
translation initiation factor 2 gamma

-
-
translation initiation factor 2 gamma
-
-
translation initiation factor 5B

-
-
translation initiation factor 5B
-
-
translation initiation factor 5B
-
-
translation initiation factor 5B
-
-
translation initiation factor 5B
-
-
translation initiation factor IF2

-
-
translation initiation factor IF2
-
-
translational GTPase

-
-
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2',3'-O-N'-methylanthranilate-GTP + H2O
2',3'-O-N'-methylanthranilate-GDP + phosphate
-
2',3'-O-N'-methylanthranilate, i.e. mant, is attached to GTP. EF-G binds and efficiently hydrolyzes mant-GTP in a ribosome-dependent manner
-
?
8-azido-GTP + H2O
8-azido-GDP + phosphate
ATP + H2O
ADP + phosphate
GTP + H2O
GDP + phosphate
GTP gamma-(p-azido)anilide + H2O
GDP + phosphoric acid p-azidoanilin
-
-
-
?
guanosine 5'-(thio)triphosphate + H2O
GDP + thiophosphate + 3 H+
guanylyl imidodiphosphate + H2O
?
ITP + H2O
IDP + phosphate
XDP + H2O
XMP + phosphate
XTP + H2O
XDP + phosphate
additional information
?
-
8-azido-GTP + H2O

8-azido-GDP + phosphate
-
-
-
?
8-azido-GTP + H2O
8-azido-GDP + phosphate
-
-
-
?
ATP + H2O

ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
GDP + H2O

?
-
-
-
?
GTP + H2O

?
-
70S ribosome, ribosome recycling factor, EF-G, GTP, 30°C, 15 min
-
r
GTP + H2O
?
kirromycin + H20
-
?
GTP + H2O
?
-
70S ribosome, ribosome recycling factor, EF-G, GTP, 30°C, 15 min
-
r
GTP + H2O

GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
IF2 in complex with GTP, but not GDP promotes fast association of ribosomal subunits during initiation. IF2 promotes fast formation of the first peptide bond in the presence of GTP, but not GDP. GTP form of IF2 accelerates formation of the 70S ribosome from subunits and GTP hydrolysis accelerates release of IF2 from the 70S ribosome
-
?
GTP + H2O
GDP + phosphate
-
importance of GTP hydrolysis in translation initiation for optimal cell growth
-
?
GTP + H2O
GDP + phosphate
-
release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Binding of GTP to RF3 and GTP hydrolysis requires peptide chain release
-
?
GTP + H2O
GDP + phosphate
-
elongation factor G
-
?
GTP + H2O
GDP + phosphate
-
elongation factor Tu
-
?
GTP + H2O
GDP + phosphate
-
the catalytic role of His84 in elongation factor Tu is to stabilize the transition state of GTP hydrolysis by hydrogen bonding to the attacking water molecule or, possibly, the gamma-phosphate group of GTP
-
?
GTP + H2O
GDP + phosphate
-
37°C
-
?
GTP + H2O
GDP + phosphate
-
the integrity of the path between the peptidyltransferase center and both GTPase-associated center and sarcin-ricin loop is important for EF-G binding
-
?
GTP + H2O
GDP + phosphate
-
0.5 mM GTP, 37°C, 10 min
-
?
GTP + H2O
GDP + phosphate
-
reaction using Escherichia coli 70S ribosomes, determination of binding of GTPases to 70S ribosomes in the GTP state, formation of 70S ribosome-tRNAPhe -GTPase-GDPNP complexes, multiple-turnover GTP hydrolysis
-
?
GTP + H2O
GDP + phosphate
after GTP hydrolysis and phosphate release, the loss of interactions between the nucleotide and the switch 1 loop of EF-Tu allows domain D1 of EF-Tu to rotate relative to domains D2 and D3 and leads to an increased flexibility of the switch 1 loop. This rotation induces a closing of the D1-D3 interface and an opening of the D1-D2 interface. The opening of the D1-D2 interface, which binds the CCA tail of the tRNA, weakens the crucial EF-Tu-tRNA interactions, which lowers tRNA binding affinity, representing the first step of tRNA release
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
reaction using Escherichia coli 70S ribosomes, determination of binding of GTPases to 70S ribosomes in the GTP state, formation of 70S ribosome-tRNAPhe -GTPase-GDPNP complexes, multiple-turnover GTP hydrolysis
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
extodomain 2+3 stimulate the GTPase activity of ectodomain 1
-
?
GTP + H2O
GDP + phosphate
-
extodomain 2+3 suppress the GTPase activity of ectodomain 1
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
GTPase activation due to C domain of the translation termination factor eRF1, which is bound with translation termination factor eRF3. As for the M and N domains, stimulation of eRF3 GTPase activity is more likely associated with the former, which is located in the large subunit along with the GTPase center of the ribosome, than with the latter, which is oriented towards the decoding center located in the small ribosomal subunit
-
?
GTP + H2O
GDP + phosphate
-
the selenocysteine tRNA-specific elongation factor is responsible for the cotranslational incorporation of selenocysteine into proteins by recoding of a UGA step codon in the presence of a downstream mRNA hairpin loop
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
two models of the reaction mechanism using the crystal structure: I. Glu81 becomes protonated upon GTP binding, with preference to bind GDP apparently contradicting its assignment as ON, or II. Glu81 protonation/deprotonation defines the ON/OFF states. Protonated Glu81, is ON, whereas X-ray(GTP):GDP is OFF. The model postulates that distant conformational changes such as domain IV rotation are uncoupled from GTP/GDP exchange and do not affect the relative GTP/GDP binding affinities. Glu81-GTP interaction helps to hold switch 2 in place, if Glu81 is deprotonated, it and nearby residues move away from their crystal positions
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
644157, 657934, 679625, 679626, 680595, 718927, 724475, 724476, 724487, 724710, 724936 -
?
GTP + H2O
GDP + phosphate
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
ir
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
60°C
-
?
GTP + H2O
GDP + phosphate
-
ribosome-dependent GTPase strongly stimulates the binding of initiator tRNA to the ribosomes even in the absence of other factors
-
?
GTP + H2O
GDP + phosphate
-
aIF2/5B enhances the translation of both leadered and leaderless mRNAs when expressed in a cell-free protein-synthesizing system
-
?
GTP + H2O
GDP + phosphate
ATP hydrolysis is insignificant compared to the levels of GTP hydrolysis
-
?
GTP + H2O
GDP + phosphate
-
displays either the intrinsic or the ribosome-dependent GTPase activity
-
?
GTP + H2O
GDP + phosphate
slow GTPase with relatively low affinity for GTP
-
?
GTP + H2O
GDP + phosphate
GTP hydrolysis by subunit aIF2gamma
-
?
GTP + H2O
GDP + phosphate
aIF2 significantly hydrolyses GTP in vitro, GTP hydrolysis by aIF2 or by its isolated gamma subunit. Assay with aIF2-Met-tRNAfMet enzyme complex and GTP
-
?
GTP + H2O
GDP + phosphate
GTP hydrolysis by subunit aIF2gamma
-
?
GTP + H2O
GDP + phosphate
aIF2 significantly hydrolyses GTP in vitro, GTP hydrolysis by aIF2 or by its isolated gamma subunit. Assay with aIF2-Met-tRNAfMet enzyme complex and GTP
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
GTP hydrolysis by subunit aIF2gamma
-
?
GTP + H2O
GDP + phosphate
aIF2 significantly hydrolyses GTP in vitro, GTP hydrolysis by aIF2 or by its isolated gamma subunit. Assay with aIF2-Met-tRNAfMet enzyme complex and GTP
-
?
GTP + H2O
GDP + phosphate
GTP hydrolysis by subunit aIF2gamma
-
?
GTP + H2O
GDP + phosphate
aIF2 significantly hydrolyses GTP in vitro, GTP hydrolysis by aIF2 or by its isolated gamma subunit. Assay with aIF2-Met-tRNAfMet enzyme complex and GTP
-
?
GTP + H2O
GDP + phosphate
GTP hydrolysis by subunit aIF2gamma
-
?
GTP + H2O
GDP + phosphate
aIF2 significantly hydrolyses GTP in vitro, GTP hydrolysis by aIF2 or by its isolated gamma subunit. Assay with aIF2-Met-tRNAfMet enzyme complex and GTP
-
?
GTP + H2O
GDP + phosphate
ATP hydrolysis is insignificant compared to the levels of GTP hydrolysis
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
slow GTPase with relatively low affinity for GTP
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
the enzyme has the same domain structure and biochemical properties of a typical IF2 species as found in bacteria or mammalian mitochondria, but with enhanced ability to bind unformylated initiator met-tRNA
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
mutant of elongation factor G containing the effector loop from Thermus aquaticus EF-Tu has markedly decreased GTPase activity and does not catalyze translocation. The loops are not functionally interchangeable since the factors interact with different states of the ribosome
-
?
GTP + H2O
GDP + phosphate
-
Base A 2660 is crucial for GTPase activity of EF-G. Reaction rates using reconstituted ribosomes, single turnover measurement, overview
-
?
GTP + H2O
GDP + phosphate
after GTP hydrolysis and phosphate release, the loss of interactions between the nucleotide and the switch 1 loop of EF-Tu allows domain D1 of EF-Tu to rotate relative to domains D2 and D3 and leads to an increased flexibility of the switch 1 loop. This rotation induces a closing of the D1-D3 interface and an opening of the D1-D2 interface. The opening of the D1-D2 interface, which binds the CCA tail of the tRNA, weakens the crucial EF-Tu-tRNA interactions, which lowers tRNA binding affinity, representing the first step of tRNA release
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
-
GDP binding structure analysis
?
GTP + H2O
GDP + phosphate
-
mutant of elongation factor G containing the effector loop from Thermus aquaticus EF-Tu has markedly decreased GTPase activity and does not catalyze translocation. The loops are not functionally interchangeable since the factors interact with different states of the ribosome
-
?
GTP + H2O
GDP + phosphate
-
elongation factor G catalyzes the translocation step in protein synthesis on the ribosome
-
?
GTP + H2O
GDP + phosphate
-
enzyme-GTP and enzyme-GDP conformations in solution are very similar. The major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome
-
?
GTP + H2O
GDP + phosphate
-
0.5 mM GTP, 37°C, 10 min
-
?
GTP + H2O
GDP + phosphate
-
EF-Tu is in its active conformation, when the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the gamma-phosphate of GTP. The activated conformation is achieved due to a critical and conserved interaction of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA. Universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome. Premature GTP hydrolysis in EF-Tu is prevented by a hydrophobic gate consisting of residues Val20 of the P loop and Ile60 of switch I, which restricts access of His84 to the catalytic water
-
?
GTP + H2O
GDP + phosphate
molecular recognition in the GTP-binding site, overview
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
EF-Tu is in its active conformation, when the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the gamma-phosphate of GTP. The activated conformation is achieved due to a critical and conserved interaction of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA. Universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome. Premature GTP hydrolysis in EF-Tu is prevented by a hydrophobic gate consisting of residues Val20 of the P loop and Ile60 of switch I, which restricts access of His84 to the catalytic water
-
?
GTP + H2O
GDP + phosphate
-
-
?
GTP + H2O
GDP + phosphate
molecular recognition in the GTP-binding site, overview
-
?
GTP + H2O
GDP + phosphate
-
GDP binding structure analysis
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
guanosine 5'-(thio)triphosphate + H2O

GDP + thiophosphate + 3 H+
-
-
-
?
guanosine 5'-(thio)triphosphate + H2O
GDP + thiophosphate + 3 H+
-
-
-
?
guanylyl imidodiphosphate + H2O

?
-
-
-
?
guanylyl imidodiphosphate + H2O
?
-
-
-
?
guanylyl imidodiphosphate + H2O
?
-
-
-
?
ITP + H2O

IDP + phosphate
-
-
-
?
ITP + H2O
IDP + phosphate
-
-
-
?
ITP + H2O
IDP + phosphate
-
-
-
?
ITP + H2O
IDP + phosphate
-
-
-
?
XDP + H2O

XMP + phosphate
-
-
-
?
XDP + H2O
XMP + phosphate
-
-
-
?
XTP + H2O

XDP + phosphate
-
-
-
?
XTP + H2O
XDP + phosphate
-
-
-
?
additional information

?
-
-
puromycin + 50S subunit {?}
-
?
additional information
?
-
-
EF4-ribosome interactions during reverse translocation, overview
-
?
additional information
?
-
-
residue 196 is located in a solvent-exposed location of the G' subdomain, while its neighboring helices AG' and BG' make contacts with protein L7/L12 of the ribosome. The latter contacts involve conserved electrostatically interacting residues that allosterically activate GTP hydrolysis in the G domain of EF-G. Residue 58 moves substantially from its initial ordered position adjacent to helix BIII
-
?
additional information
?
-
-
EF-G binding, without GTP hydrolysis, promotes slow and possibly incomplete translocation
-
?
additional information
?
-
enzyme-ribosome binding analysis, overview. Binding of wild-type EF4 and mutant variants to the ribosome in the presence of guanine nucleotides, kinetics and affinities
-
?
additional information
?
-
apo-form, and GDP- and nonhydrolysable GTP analogue guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA, structure analysis, overview
-
-
additional information
?
-
contacts between EF-G, protein S12, and helices 43 and 44 of 23S ribosomal RNA. Escherichia coli strain MRE600 70S ribosomes are used as substrates
-
-
additional information
?
-
formation of the 70S-fMet-tRNAi Met-IF2-GDPNP complex. 70S ribosomes are isolated from Escherichia coli strain CAN20, recombinant His-tagged IF2 enzyme, non-hydrolyzable GTP analogue GDPNP
-
-
additional information
?
-
-
formation of the 70S-fMet-tRNAi Met-IF2-GDPNP complex. 70S ribosomes are isolated from Escherichia coli strain CAN20, recombinant His-tagged IF2 enzyme, non-hydrolyzable GTP analogue GDPNP
-
-
additional information
?
-
IF2 has protein chaperone activity. It catalyzes the refolding of heat-denatured GFP upon incubation for 8 min at 25°C at chaperone/GFP stoichiometric ratios of 1:1 carried out in buffer containing 1 mM GTP and 1 mM ATP. IF2alpha displays the highest chaperone activity in the presence of GTP, and its activity is substantially reduced, albeit not completely abolished, in the presence of GDP, or of the non-hydrolysable analogue GDPCP or in the absence of guanine nucleotides
-
-
additional information
?
-
-
IF2 has protein chaperone activity. It catalyzes the refolding of heat-denatured GFP upon incubation for 8 min at 25°C at chaperone/GFP stoichiometric ratios of 1:1 carried out in buffer containing 1 mM GTP and 1 mM ATP. IF2alpha displays the highest chaperone activity in the presence of GTP, and its activity is substantially reduced, albeit not completely abolished, in the presence of GDP, or of the non-hydrolysable analogue GDPCP or in the absence of guanine nucleotides
-
-
additional information
?
-
upon GTP hydrolysis, phosphate release results in a loss of the switch 1 loop anchoring to the rest of D1, which frees D1 to rotate around the switch 2 helix. This rotation closes the D1-D3 interface and opens the D2-D3 interface, possibly decreasing the interaction of EF-Tu with the amino acid and the CCA tail of the tRNA and, therefore, the affinity of the tRNA to EF-Tu
-
-
additional information
?
-
-
EF4-ribosome interactions during reverse translocation, overview
-
?
additional information
?
-
elongation factor eEF2 catalyzes ribosomal reverse translocation at one mRNA triplet. This process requires a cognate tRNA in the ribosomal E-site and cannot occur spontaneously without eEF2. The efficiency of this reaction depends on the concentrations of eEF2 and cognate tRNAs and increases in the presence of nonhydrolyzable GTP analogues. Deacylated tRNAHis, cognate to the E-site codon, to the POST ribosomal complexes along with eEF2-GTP, causes a shift of the main toeprint peak by 3 nt toward the 5' end of the mRNA. POST ribosomes relocate backwards by three nucleotides in the presence of cognate deacylated tRNA and eEF2. Reverse translocation required up to a 20fold excess of eEF2 over the ribosomal complexes, whereas direct translocation is effective at a 2:1 ratio. Model of eEF2-catalyzed reverse translocation, overview
-
-
additional information
?
-
substrate eIF2, phosphorylation of the eIF2alpha subunit in response to various cellular stresses converts substrate eIF2 into a competitive inhibitor of eIF2B, which triggers the integrated stress response (ISR)
-
-
additional information
?
-
-
GTP/GDP binding analysis using molecular dynamics and a continuum electrostatic free energy method
-
?
additional information
?
-
aIF2 shows very high conformational flexibility in the alpha- and beta-subunits probably required for interaction of aIF2 with the small ribosomal subunit, overview
-
?
additional information
?
-
-
aIF2 shows very high conformational flexibility in the alpha- and beta-subunits probably required for interaction of aIF2 with the small ribosomal subunit, overview
-
?
additional information
?
-
-
EF-1alpha shows GTPase activity and GDP-binding ability
-
?
additional information
?
-
-
HflX interacts with 50S and 70S particles, and also with the 30S subunit, independent of the nucleotide-bound state and in tight binding, minimal model for the functional cycle of HflX, interaction with the 70S ribosome and functional mechanism of HflX, overview
-
?
additional information
?
-
-
structure-activity relationship, molecular dynamics simulations, overview
-
?
additional information
?
-
-
the enzyme exhibits significant binding activity with the nonformylated Met-tRNAf(Met)
-
?
additional information
?
-
-
eIF2A functions as a suppressor of Ure2p internal ribosome entry site-mediated translation in yeast cells
-
?
additional information
?
-
-
Met-tRNA + 40S ribosomal subunit {?}
-
?
additional information
?
-
-
Met-tRNA + 40S ribosomal subunit {?}
-
?
additional information
?
-
-
feeding artificial milk diets stimulate protein synthesis in skeletal muscle and liver of neonatal pigs by modulating the translation initiation factors that regulate mRNA binding to the ribosomal complex. However, provision of a high-protein diet that exceeds the protein requirement does not further enhance protein synthesis or translation initiator factor activation
-
?
additional information
?
-
upon GTP hydrolysis, phosphate release results in a loss of the switch 1 loop anchoring to the rest of D1, which frees D1 to rotate around the switch 2 helix. This rotation closes the D1-D3 interface and opens the D2-D3 interface, possibly decreasing the interaction of EF-Tu with the amino acid and the CCA tail of the tRNA and, therefore, the affinity of the tRNA to EF-Tu
-
-
additional information
?
-
the G-nucleotide binding pocket includes five G motifs (G1-G5) that are conserved in trGTPase factors. In the ribosome-bound EF4, the G1 motif (residues 18-24) establishes extensive contacts with the triphosphate moiety and ribose sugar of GDPCP. EF4 GTPase activation upon ribosome binding
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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BaCl2
-
10 mM, about 8fold stimulation
CaCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
CoCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
MgCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
MnCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
NaCl
-
GTPase activity is measured in the presence of 3.6 M NaCl
SrCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
Zn2+
zinc-binding domain in the beta-subunit
Mg2+

-
required
Mg2+
required for catalysis
Mg2+
-
plays a marginal role in the nucleotide exchange process
Mg2+
requires Mg2+ for its full GTPase catalytic activity
Mg2+
-
GTPase bound to Mg2+GDP reveals two new binding conformations. In the first the protein undergoes a conformational change that brings a conserved aspartate into its second coordination sphere. In the second, the magnesium coordination sphere is disrupted so that only five oxygen ligands are present
Mg2+
required, binding tructure analysis
Mn2+

-
-
Na+

-
-
additional information

decreased gene expression of A1, A2, A3 and A4 gene under iron deficiency
additional information
decreased gene expression of A1, A2, A3 and A4 gene under iron deficiency
additional information
decreased gene expression of A1, A2, A3 and A4 gene under iron deficiency
additional information
decreased gene expression of A1, A2, A3 and A4 gene under iron deficiency
additional information
-
decreased gene expression of A1, A2, A3 and A4 gene under iron deficiency
additional information
high concentrations of Mg2+ and spermidine doe not induce spontaneous reverse translocation, as has been reported
additional information
-
GTPase stimulated by ethylene glycol and BaCl2 does not require the presence of univalent cations. Li+, Na+, K+ or NH4+ added singularly up to 1 M concentration, do not produce any significant stimulation of SsEF-2 GTPase either in the absence or in the presence of ethylene glycol. They reduce the stimulation of SsEF-2 GTPase by ethylene glycol plus BaCl2 or SrCl2
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Adenyl-5'-yl imidodiphosphate
Anti-EF-Tu antibody
-
-
-
cycloheximide
added to the POST complexes in the presence of eEF2 and deacylated tRNAHis, it blocks the -3 nt shift that supports the reverse translocation model
EF-G GTPase inhibitor
-
-
-
GE2270A
-
antibiotic inhibits intrinsic GTPase and that stimulated by ribosomes; thiazolyl-peptide antibiotic, inhibits both the intrinsic GTPase of elongation factor 1alpha and that stimulated by ribosomes. The M domain is the region of the enzyme most responsible for the interaction with GE2270A
guanidine hydrochloride
-
deactivation by denaturation of the protein
guanosine 5'-(beta,gamma-imido)triphosphate
-
-
guanosine 5'-tetraphosphate
-
competitive inhibition of intrinsic GTPase, inhibition of archaeal protein synthesis in vitro, even though the concentration required to get inhibition is higher than that required for the eubacterial and eukaryal systems
guanosine-5'-[(beta,gamma)-imido]triphosphate
-
i.e. GppNHp. GTPase activity in the presence of a molar concentration of NaCl is competitively inhibited
guanyl-5'-yl imidodiphosphate
guanyl-5'-yl imidotriphosphate
-
-
guanyl-5'yl-imidodiphosphate
-
-
H2O2
oxidation of EF-G inhibits the function of EF-G on the ribosome. With hydrogen peroxide, neither the insertion of EF-G into the ribosome nor single-cycle translocation activity in vitro is affected, while the GTPase activity and the dissociation of EF-G from the ribosome are suppressed when EF-G is oxidized. The synthesis of longer peptides is suppressed to a greater extent than that of a shorter peptide when EF-G is oxidized
hygromycin B
the antibiotic effectively inhibits translocation of mRNA and tRNAs on the ribosome in both bacteria and eukaryotes. Hygromycin B blocks the toeprint shift induced by eEF2 and deacylated tRNA
NH4Cl
-
at higher concentration
P3-1-(2-nitro)phenylethylguanosine 5'-O-triphosphate
-
-
phosphorylated eIF2
IF2alpha is phosphorylated at Ser51 by four kinases in what is collectively known as the integrated stress response (ISR). Phosphorylation of the eIF2alpha subunit in response to various cellular stresses converts eIF2-GDP into a competitive inhibitor of eIF2B, which triggers the integrated stress response (ISR)
-
purine and pyrimidine nucleotides
tetracycline
-
mixed inhibition. The inhibition level depends on the antibiotic concentration, even though a complete inhibition is not reached even in the presence of 0.120 mM antibiotic, a concentration corresponding to about 200fold molar excess over the elongation factor
translation initiation factor IF1
-
-
-
translation initiation factor IF3
-
inhibition could be overcome by increasing concentrations of divalent cations
-
Urea
-
deactivation by denaturation of the protein
Adenyl-5'-yl imidodiphosphate

-
-
Adenyl-5'-yl imidodiphosphate
-
-
enacylotoxin IIa

-
-
-
Fusidic acid

-
inhibition of ribosome disassembly by EF-G and ribosome recycling factor, no influence on GTP hydrolysis
Fusidic acid
a specific inhibitor of the GTPase activity of EF-G, almost complete inhibition
GDP

-
-
GDP
-
competitive with GTP
GDP
-
GTPase activity in the presence of a molar concentration of NaCl is competitively inhibited
guanyl-5'-yl imidodiphosphate

-
competitive with GTP
guanyl-5'-yl imidodiphosphate
-
-
guanyl-5'-yl imidodiphosphate
-
-
kirromycin

KIR, an antibiotic that directly binds to the interface of EF-Tu domains D1 and D3 and prevents dissociation of EF-Tu from the ribosome and from the amino acid-tRNA after GTP hydrolysis. Kirromycin binds within the D1-D3 interface, sterically blocking its closure, but does not prevent hydrolysis. With KIR bound, the overall conformation of EF-Tu remains close to the GTP-bound conformation after hydrolysis, both on and off the ribosome
kirromycin
KIR, an antibiotic that directly binds to the interface of EF-Tu domains D1 and D3 and prevents dissociation of EF-Tu from the ribosome and from the amino acid-tRNA after GTP hydrolysis. Kirromycin binds within the D1-D3 interface, sterically blocking its closure, but does not prevent hydrolysis. With KIR bound, the overall conformation of EF-Tu remains close to the GTP-bound conformation after hydrolysis, both on and off the ribosome
N-ethylmaleimide

-
-
ppGpp

-
-
pulvomycin

-
-
pulvomycin
-
the antibiotic is able to reduce in vitro the rate of protein synthesis however, the concentration of pulvomycin leading to 50% inhibition (173 mM) is two order of magnitude higher but one order lower than that required in eubacteria and eukarya, respectively. Pulvomycin is able to decrease the affinity of the elongation factor toward aa-tRNA only in the presence of GTP, to an extent similar to that measured in the presence of GDP
purine and pyrimidine nucleotides

-
-
purine and pyrimidine nucleotides
-
-
Thiostrepton

-
inhibits the ribosome-stimulated GTPase activity of EF-G and EF4. An EF-G mutant lacking domains 4 and 5 is insensitive to the effects of thiostrepton on both GTPase activity and ribosome binding
Thiostrepton
inhibits the stimulation of the enzyme's GTPase activity by the 70S ribosome
vanadate

-
inhibition of ribosome disassembly, no influence on GTP hydrolysis
additional information

-
viomycin and fusidic acid do not prevent GTP hydrolysis, but these antibiotics trap EF-G on the ribosome before or after ribosomal translocation, respectively
-
additional information
-
in free enzyme EF-G, crucial sensors of switch I and II regions are disordered and become ordered in the complex with a nonhydrolyzable GTP analogue, GDPCP, on the ribosome. This causes a reorientation of EF-G such that the tip of domain IV moves and the CHI state ofthe ribosome is stabilized
-
additional information
ADP-ribosylation of eEF2 domain IV blocks reverse translocation activity of eEF2. ADP-ribosylation may directly interrupt the ability of eEF2 to stabilize the intermediate conformation of the tRNA ends during their movement through the SSU in the course of translocation
-
additional information
-
subunit alpha, beta and delta of eIF2B down-regulates activity of the eIF2B catalytic subcomplex
-
additional information
subunit alpha, beta and delta of eIF2B down-regulates activity of the eIF2B catalytic subcomplex
-
additional information
-
ribosomes lacking the 23S rRNA and with deletion of SRL region, but not of GAC, inactivate EF-G1
-
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1-propanol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
2-propanol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
50S ribosome
stimulates the enzyme
-
70S ribosome
required, stimulates the enzyme
-
eIF1A
GTPase-activating protein (GAP) for eIF2, the interaction is mediated by an eIF5B-binding motif located at the C-terminus of eIF1A. The C-terminal tail of eIF1A is located in the ribosomal P-site and counteracts the transition from open to closed complex. EIF5 competes with eIF1A for binding to eIF5B
-
ethanol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
ethylene glycoI
-
60%, 300fold stimulation
glycerol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
GMP-PCP
non-hydrolyzable or slowly hydrolyzable GTP analogues such as GMP-PCP and GMP-PNP, able to stall elongation factor on the ribosome, increase the efficiency of the reverse translocation reaction
-
GMP-PNP
non-hydrolyzable or slowly hydrolyzable GTP analogues such as GMP-PCP and GMP-PNP, able to stall elongation factor on the ribosome, increase the efficiency of the reverse translocation reaction
methanol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
pulvomycin
-
increasing pulvomycin concentration increased the rate of the intrinsic GTPase catalysed by elongation factor 1alpha, reaching its maximum stimulation effect at 30 mM. Pulvomycin exerts its stimulatory function at all the tested temperatures (45-75°C).
eIF5

eIF5 is the GTPase-activating protein (GAP) of eIF2, eIF5 promotes GTP hydrolysis by eIF2, followed by phosphate release. EIF2-GDP has lower affinity for Met-tRNAi than eIF2-GTP, and is released together with its GAP, eIF5
-
eIF5
human eIF5, the GTPase-activating protein (GAP) for eIF2, also binds to eIF5B, with affinity that is about two orders of magnitude higher than that of eIF1A. The interaction is mediated by an eIF5B-binding motif located at the C-terminus of eIF5, similar to that of eIF1A and the two proteins compete for binding to eIF5B. NMR structure analysis of the binding interface between eIF5-CT39 and eIF5B-D4, structure of the human eIF5B-D4-eIF5-C-terminal tail (CTT) complex, overview
-
kirromycin

-
-
kirromycin
-
enhances activity of mutant enzyme G13A (maximal stimulation at 0.04 mM), does not stimulate intrinsic GTPase of SsEF-1alpha triggered by 3.6 M NaCl
L7/12

-
functional compatibility between elongation factor G and the L7/12 protein in the ribosome governs its translational specificity
-
L7/12
-
the C-terminal domian of L7/12 is responsible for EF-Tu function. Functional compatibility between elongation factor Tu and the L7/12 protein in the ribosome governs its translational specificity
-
NaCl

-
-
NaCl
-
intrinsic GTPase activity of elongation factor 1alpha is triggered in vitro by NaCl at molar concentrations. The sodium ion is responsible for the induction of the GTPase activity, whereas the anion modulates the enzymatic activity through destabilization of particular regions of the protein
NaCl
-
intrinsic GTPase activity that is triggered in vitro by NaCl at molar concentrations
ribosomal subunits

-
-
-
ribosome

-
stimulates GTPase activity of elongation factor Tu. The factor binding site is loacetd on the 50S ribosomal subunit and comprises proteins L7/12, L10, L11, the l11-binding region of 23 rRNA, and the sarcin-ricin loop of 23S rRNA. L7/12 stimulates the GTPase activity of elongation factor G by inducing the catalytically active conformation of the G domain
-
ribosome
-
stimulates GTPase activity of elongation factor Tu. The factor binding site is loacetd on the 50S ribosomal subunit and comprises proteins L7/12, L10, L11, the l11-binding region of 23 rRNA, and the sarcin-ricin loop of 23S rRNA. L7/12 stimulates the GTPase activity of elongation factor Tu by inducing the catalytically active conformation of the G domain
-
streptomycin

-
-
additional information

activity triggered by ribosome-induced conformational changes of EF-Tu
-
additional information
-
activity triggered by ribosome-induced conformational changes of EF-Tu
-
additional information
the 30S ribosome does not stimulate the enzyme
-
additional information
conserved residue His91 plays a direct role in the switch II loop of EF-G in GTPase activation
-
additional information
GTP hydrolysis by EF-G gets strongly stimulated by the ribosome
-
additional information
the GTPase activity of LepA, like that of other translational GTPases, is stimulated by interactions with both subunits of the ribosome
-
additional information
evolutionary conservation of the eIF5B-binding motif in eIF1A and eIF5
-
additional information
evolutionary conservation of the eIF5B-binding motif in eIF1A and eIF5
-
additional information
-
evolutionary conservation of the eIF5B-binding motif in eIF1A and eIF5
-
additional information
presence of nonhydrolyzable GTP analogues increases the reverse translocation at mRNA activity of eukaryotic elongation factor eEF2. Reverse translocation requires an excessive concentration of cognate deacylated tRNA
-
additional information
-
phosphorylation
-
additional information
phosphorylation
-
additional information
-
active in GTP-bound form, inactive in GDP-bound form
-
additional information
active in GTP-bound form, inactive in GDP-bound form
-
additional information
-
GTP hydrolysis is essential for release of eIF5B from the 80S ribosomal subunit
-
additional information
active in GTP-bound form, inactive in GDP-bound form
-
additional information
active in GTP-bound form, inactive in GDP-bound form
-
additional information
EF4 GTPase activation upon ribosome binding
-
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additional information
additional information
-
0.12
ATP

-
-
0.00032
GTP

recombinant wild-type enzyme in presence of 70S ribosome, pH 7.5, 37°C
0.0008
GTP
-
mutant A26G, pH 7.5, 60°C, presence of 40% ethylene glycol
0.0009
GTP
-
pH 7.8, 50°C
0.0009
GTP
SsMT4EF-1alpha
0.001
GTP
-
wild-type, pH 7.5, 60°C, presence of 40% ethylene glycol
0.0012
GTP
-
pH 7.8, 60°C
0.0013
GTP
-
pH 7.8, 80°C
0.0014
GTP
-
pH 7.8, 70°C
0.002 - 0.009
GTP
-
depending on NaCl-concentration and temperature
0.0023
GTP
-
truncated mutant, domains G+M, 60°C, pH 7.8
0.0023
GTP
-
Ss(GM)EF-1alpha
0.0024
GTP
-
truncated mutant, domain G, 60°C, pH 7.8
0.0024
GTP
-
Ss(G)EF-1alpha
0.0025
GTP
-
pH 7.8, 60°C
0.0025
GTP
-
wild-type, 60°C, pH 7.8
0.0027
GTP
-
60°C, wild-type enzyme
0.0027
GTP
SsMT3EF-1alpha
0.00436
GTP
-
pH 7.8, 50°C, GTPase activity in the presence 3.6 M NaCl
0.0046
GTP
-
60°C, mutant enzyme G13A
0.0053
GTP
pH 7.5, 50°C, wild-type enzyme
0.0053
GTP
-
pH 7.8, 87°C
0.0053
GTP
pH 7.4, 50°C, in absence of ribosomes
0.0055
GTP
-
mutant A26G, pH 7.5, 60°C, presence of 10% ethylene glycol
0.0075
GTP
-
pH 7.5, 60°C
0.0081
GTP
in presence of 70S ribosome, H91E, pH 7.5, 37°C
0.0082
GTP
in presence of 70S ribosome, wild-type enzyme, pH 7.5, 37°C
0.0085
GTP
in presence of 70S ribosome, F94L, pH 7.5, 37°C
0.0096
GTP
-
wild-type, pH 7.5, 60°C, presence of 10% ethylene glycol
0.0106
GTP
in presence of 70S ribosome, H91A, pH 7.5, 37°C
0.011
GTP
pH 7.5, 50°C, mutant enzyme F236P
0.0129
GTP
pH 7.8, 50°C, N-terminal deletion mutant
0.0134
GTP
in presence of 70S ribosome, H91Q, pH 7.5, 37°C
0.0141
GTP
pH 7.8, 50°C, full-length enzyme
0.0143
GTP
in presence of 70S ribosome, H91R, pH 7.5, 37°C
0.0194
GTP
-
mutant A26G, pH 7.5, 60°C
0.0532
GTP
-
pH 7.8, 95°C
0.27
GTP
recombinant wild-type enzyme in absence of 70S ribosome, pH 7.5, 37°C
additional information
additional information

-
pre-steady-state kinetic analysis of HflX and Hflx ribosomal complexes interacting with GDP and a nonhydrolyzable analogue of mant-GTP, overview
-
additional information
additional information
-
ribosome binding kinetics of GTP hydrolysis-inactive recombinant EF-G mutants 58C and 196C labeled with 2',7'-difluorofluorescein maleimide, i.e. 58C-mant and 196C-mant, overview
-
additional information
additional information
substrate and product binding kinetics and thermodynamics with ON and OFF aIF2 , overview
-
additional information
additional information
-
substrate and product binding kinetics and thermodynamics, overview
-
additional information
additional information
-
substrate binding kinetics of wild-type and mutant IF2s, overview
-
additional information
additional information
Michaelis-Menten kinetics of GTP hydrolysis, stopped flow measurements, kinetic analysis of wild-type and mutant enzymes, overview
-
additional information
additional information
-
thermodynamics of nucleotide binding
-
additional information
additional information
GTP hydrolysis kinetics of wild-type and mutant enzyme subunits
-
additional information
additional information
isothermal titration calorimetry and kinetics at 20°C, binding energetics of Efl1 to guanine nucleotides, overview
-
additional information
additional information
-
isothermal titration calorimetry and kinetics at 20°C, binding energetics of Efl1 to guanine nucleotides, overview
-
additional information
additional information
single-turnover GTP hydrolysis kinetics by mixing 70S ribosomes and [3H]GTP with EF-G
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0004
GTP

pH 7.5, 50°C, wild-type enzyme
0.00053
GTP
pH 7.5, 50°C, mutant enzyme F236P
0.00092
GTP
pH 7.4, 50°C, in absence of ribosomes
0.001
GTP
-
Ss(G)EF-1alpha
0.00105
GTP
pH 7.8, 50°C, full-length enzyme
0.00167
GTP
-
60°C, mutant enzyme G13A
0.003
GTP
-
pH 7.8, 50°C, GTPase activity in the presence 3.6 M NaCl
0.003
GTP
recombinant wild-type enzyme in absence of 70S ribosome, pH 7.5, 37°C
0.0033
GTP
-
wild-type, pH 7.5, 60°C, presence of 10% ethylene glycol
0.01
GTP
-
truncated mutant, domain G, 60°C, pH 7.8
0.013
GTP
-
60°C, wild-type enzyme
0.014
GTP
-
wild-type, 60°C, pH 7.8
0.018
GTP
-
truncated mutant, domains G+M, 60°C, pH 7.8
0.018
GTP
-
Ss(GM)EF-1alpha
0.026
GTP
pH 7.8, 50°C, N-terminal deletion mutant
0.032
GTP
-
wild-type, pH 7.5, 60°C, presence of 40% ethylene glycol
0.12
GTP
-
mutant A26G, pH 7.5, 60°C, presence of 10% ethylene glycol
0.133
GTP
-
mutant A26G, pH 7.5, 60°C
0.165
GTP
-
mutant A26G, pH 7.5, 60°C, presence of 40% ethylene glycol
1.9
GTP
in presence of 70S ribosome, H91E, pH 7.5, 37°C
2 - 8
GTP
in presence of 70S ribosome, H91A, pH 7.5, 37°C
2 - 8
GTP
recombinant enzyme EF-G mutant H91A, pH 7.5, 37°C
2.3
GTP
recombinant wild-type enzyme in presence of 70S ribosome, pH 7.5, 37°C
27
GTP
in presence of 70S ribosome, H91R, pH 7.5, 37°C
170
GTP
in presence of 70S ribosome, F94L, pH 7.5, 37°C
174
GTP
in presence of 70S ribosome, H91Q, pH 7.5, 37°C
202
GTP
in presence of 70S ribosome, wild-type enzyme, pH 7.5, 37°C
202
GTP
wild-type enzyme EF-G, pH 7.5, 37°C
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