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Literature summary extracted from

  • Simonetti, A.; Marzi, S.; Fabbretti, A.; Hazemann, I.; Jenner, L.; Urzhumtsev, A.; Gualerzi, C.O.; Klaholz, B.P.
    Structure of the protein core of translation initiation factor 2 in apo, GTP-bound and GDP-bound forms (2013), Acta Crystallogr. Sect. D, 69, 925-933.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.5.3 recombinant expression of nontagged wild-type full-length enzyme in Escherichia coli strain BL21(DE3) and of selenomethionine-labelled enzyme in Escherichia coli strain B834 (DE3) Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.5.3 purified recombinant apoenzyme protein core and enzyme in complex with GTP or GDP, sitting-drop vapour diffusion method, mixing of protein in 20 mM HEPES, pH 7.5, 50 mM KCl, 20 mM MgCl2, 1 mM DTT, with 2.5% glycerol and with reservoir solution containing 20% PEG 3350 and 0.2 M ammonium nitrate, to a final volume of 0.008 ml, 21°C, 1-3 weeks, X-ray diffraction structure determination and analysis Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.5.3 Mg2+ required, binding tructure analysis Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.5.3 GTP + H2O Thermus thermophilus
-
 GDP + phosphate
-
 ?
3.6.5.3 GTP + H2O Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 GDP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.5.3 Thermus thermophilus P48515
-
-
3.6.5.3 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 P48515
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.5.3 recombinant wild-type and selenomethionine-labelled enzymes from Escherichia coli by hydrophobic interaction chromatography Thermus thermophilus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.6.5.3 GTP + H2O = GDP + phosphate conformational changes of the protein upon nucleotide binding, in particular in the P-loop region, which extend to the functionally relevant switch II region. The latter carries a catalytically important and conserved histidine residue which is observed in different conformations in the GTP and GDP complexes. Activation of GTP hydrolysis may occur by a conformational repositioning of the histidine residue Thermus thermophilus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.5.3 GTP + H2O
-
 Thermus thermophilus GDP + phosphate
-
 ?
3.6.5.3 GTP + H2O molecular recognition in the GTP-binding site, overview Thermus thermophilus GDP + phosphate
-
 ?
3.6.5.3 GTP + H2O
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 GDP + phosphate
-
 ?
3.6.5.3 GTP + H2O molecular recognition in the GTP-binding site, overview Thermus thermophilus HB8 / ATCC 27634 / DSM 579 GDP + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.5.3 trimer
-
 Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
3.6.5.3 IF2
-
 Thermus thermophilus
3.6.5.3 translation initiation factor 2
-
 Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.5.3 7.5
-
 assay at Thermus thermophilus

General Information

EC Number General Information Comment Organism
3.6.5.3 additional information conformational changes of enzyme IF2 upon nucleotide binding control switches I and II in the G domain, modeling, overview Thermus thermophilus
3.6.5.3 physiological function the translation initiation factor 2 (IF2) is involved in the early steps of bacterial protein synthesis. It promotes the stabilization of the initiator tRNA on the 30S initiation complex and triggers GTP hydrolysis upon ribosomal subunit joining Thermus thermophilus