Information on EC 2.1.1.170 - 16S rRNA (guanine527-N7)-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.170
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RECOMMENDED NAME
GeneOntology No.
16S rRNA (guanine527-N7)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine527 in 16S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (guanine527-N7)-methyltransferase
The enzyme specifically methylates guanine527 at N7 in 16S rRNA.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 168
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-
Manually annotated by BRENDA team
strain 168
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-
Manually annotated by BRENDA team
strain BW25113
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-
Manually annotated by BRENDA team
strain A3(2)
SwissProt
Manually annotated by BRENDA team
strain A3(2)
SwissProt
Manually annotated by BRENDA team
IFO13189
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-
Manually annotated by BRENDA team
strain HB8
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
RsmG is an S-adenosyl-L-methionine-dependent methyltransferase responsible for the synthesis of m7G527 in the 530 loop of bacterial 16S rRNA. This loop is universally conserved, plays a key role in ribosomal accuracy, and is a target for streptomycin binding, mechanisms controlling RsmG expression and activity, overview. Gene rsmG as part of a bicistronic operon also has its own promoter, which appears, in actively growing cells, as a control device to offset both the relatively low stability of RsmG and inhibition of the operon promoter. Critical importance of some residues located in the active site of Escherichia coli RsmG for the m7G modification process, the residues play a role in rRNA binding and catalysis
additional information
positively charged residues on the protein surface around the active site, K100/R101, R123, K165, and R197, might play a role in the binding of the incoming 530 loop since their change to alanine impairs the modification function of RsmG
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the 30S subunits in their native conformation are not a proper substrate and removal of Mg2+ ions from the subunit is required to open the structure sufficiently to expose elements involved in enzyme binding
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
activity of rsmGp slightly increases by fourfold when cells are grown in minimal media supplemented with glycerol instead of glucose
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
activity of rsmGp slightly increases by fourfold when cells are grown in minimal media supplemented with glycerol instead of glucose
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23840
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MALDI-MS
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 23842, MALDI-MS
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor diffusion at 4°C against a reservoir containing 0.1 M of sodium citrate pH 6.5, 15% polyethylene glycol 4000, and 10% isopropanol
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microbatch technique under oil at 4°C. Determination of the structure of RsmG (249 amino acids) in three different crystal forms: the enzyme in complex with the cofactor S-adensosyl-L-methionine, the enzyme in complex with S-adenosyl-L-homocysteine, the enzyme in complex with adenosine monophosphate and S-adenosyl-L-methionine. RsmG X-ray crystal structures at up to 1.5 A resolution. Cofactor-bound crystal structures of RsmG reveals a positively charged surface area remote from the active site that binds an adenosine monophosphate molecule
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant FLAG-tagged RsmG from Escherichia coli TOP10 cells by affinity chromatography
the AdoMet cofactor is tightly bound in RsmG and copurifies with the recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli BL21
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gene rsmG is the second member in a bicistronic operon, rsmG also has its own promoter, RsmG expression might depend on the activity of an inverted repeated region, located between the rsmG promoter and ribosome binding site, which works as a weak transcriptional terminator. Expression of C-terminally His6-tagged and FLAG-tagged RsmG in Escherichia coli TOP10 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RsmG levels decrease under conditions that down-regulate rRNA synthesis, but coordination between rRNA and RsmG expression does not seem to occur at the level of transcription initiation
slight induction of rsmGp during stationary phase is independent of the stress-inducible sigma factor RpoS
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D56A
site-directed mutagenesis of the catalytic residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
D71A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
D96A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
G73A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-sensitive and shows reduced activity compared to the wild-type enzyme
G77A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
H53A
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
K100A/R101A
site-directed mutagenesis of the RNA-binding residues, the mutant is streptomycin-resistant and catalytically inactive
K165A
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
N39A
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inactive
P79A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
R123A
site-directed mutagenesis of the RNA-binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
R139A
site-directed mutagenesis of the catalytic residue, the mutant is streptomycin-resistant and catalytically inactive
R139K
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
R197A
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
additional information
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