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Literature summary for 3.6.5.3 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
Search for more literature for 3.6.5.3

Cloned(Commentary)

Cloned (Comment) Organism
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)

Crystallization (Comment) Organism
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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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)

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

Subunits

Subunits Comment Organism
trimer
-
 Thermus thermophilus

Synonyms

Synonyms Comment Organism
IF2
-
 Thermus thermophilus
translation initiation factor 2
-
 Thermus thermophilus

pH Optimum

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

General Information

General Information Comment Organism
additional information conformational changes of enzyme IF2 upon nucleotide binding control switches I and II in the G domain, modeling, overview Thermus thermophilus
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