Tr-type G domain, conserved site
Short name | G_TR_CS |
Description
* Prokaryotic initiation factor 2 (IF2) and the related eukaryotic initiation factor 5B (eIF5B), catalyze ribosomal subunit joining to form elongation- competent ribosomes
* Bacterial SelB and eukaryotic/archaeal gamma subunit of initiation factor 2 (eIF-2gamma), specifically recognise noncanonical tRNAs. SelB specifically recognises selenocysteylated tRNA(Sec) and eIF-2gamma initiator tRNA (Met-tRNA(i))
* Bacterial elongation factor Tu (EF-Tu) and its archaeal and eukaryotic counterpart elongation factor 1 (EF-1 alpha), bring the aminoacyl-tRNA into the A site of the ribosome
* Bacterial peptide elongation factor G (EF-G) and its counterpart in Eukarya and Archaea, EF-2, catalyse the translocation step of translation
References
1.Classification and evolution of P-loop GTPases and related ATPases. Leipe DD, Wolf YI, Koonin EV, Aravind L. J. Mol. Biol. 317, 41-72, (2002). View articlePMID: 11916378
2.Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases. Eiler D, Lin J, Simonetti A, Klaholz BP, Steitz TA. Proc. Natl. Acad. Sci. U.S.A. 110, 15662-7, (2013). View articlePMID: 24029018
3.eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining. Kuhle B, Ficner R. EMBO J. 33, 1177-91, (2014). View articlePMID: 24686316
4.Evolutionary relationship between translation initiation factor eIF-2gamma and selenocysteine-specific elongation factor SELB: change of function in translation factors. Keeling PJ, Fast NM, McFadden GI. J. Mol. Evol. 47, 649-55, (1998). View articlePMID: 9847405
5.Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors. Leibundgut M, Frick C, Thanbichler M, Bock A, Ban N. EMBO J. 24, 11-22, (2005). View articlePMID: 15616587
6.Structure-based sequence alignment of elongation factors Tu and G with related GTPases involved in translation. Avarsson A. J. Mol. Evol. 41, 1096-104, (1995). PMID: 8587108
7.Lateral transfer of an EF-1alpha gene: origin and evolution of the large subunit of ATP sulfurylase in eubacteria. Inagaki Y, Doolittle WF, Baldauf SL, Roger AJ. Curr. Biol. 12, 772-6, (2002). View articlePMID: 12007424
8.The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. al-Karadaghi S, Aevarsson A, Garber M, Zheltonosova J, Liljas A. Structure 4, 555-65, (1996). View articlePMID: 8736554
9.A computational study of elongation factor G (EFG) duplicated genes: diverged nature underlying the innovation on the same structural template. Margus T, Remm M, Tenson T. PLoS ONE 6, e22789, (2011). View articlePMID: 21829651
Cross References
Contributing Member Database Entry
- PROSITE patterns:PS00301