InterPro : IPR004540

Name  Translation elongation factor EFG/EF2 Short Name  Transl_elong_EFG/EF2
Type  Family Description  Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [, , ]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution.EF-G is a large, five-domain GTPase that promotes the directional movement of mRNA and tRNAs on the ribosome in a GTP-dependent manner. Unlike other GTPases, but by analogy to the myosin motor, EF-G performs its function of powering translocation in the GDP-bound form; that is, in a kinetically stable ribosome-EF-G(GDP) complex formed by GTP hydrolysis on the ribosome. The complex undergoes an extensive structural rearrangement, in particular affecting the small ribosomal subunit, which leads to mRNA-tRNA movement. Domain 4, which extends from the 'body' of the EF-G molecule much like a lever arm, appears to be essential for the structural transition to take place. In a hypothetical model, GTP hydrolysis induces a conformational change in the G domain of EF-G, which affects the interactions with neighbouring domains within EF-G. The resulting rearrangement of the domains relative to each other generates conformational strain in the ribosome to which EF-G is fixed. Because of structural features of the tRNA-ribosome complex, this conformational strain results in directional tRNA-mRNA movement. The functional parallels between EF-G and motor proteins suggest that EF-G differs from classical G-proteins in that it functions as a force-generating mechanochemical device rather than a conformational switch [].Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homologue to canonical (e.g. Escherichia coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis sp.(strain PCC 6803)has a few proteins more closely related to EF-G than to any other characterised protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

8 Contains

Id Name Short Name Type
IPR009022 Elongation factor G, III-V domain EFG_III-V Domain
IPR000640 Translation elongation factor EFG, V domain EFG_V Domain
IPR009000 Translation protein, beta-barrel domain Transl_B-barrel Domain
IPR020568 Ribosomal protein S5 domain 2-type fold Ribosomal_S5_D2-typ_fold Domain
IPR004161 Translation elongation factor EFTu/EF1A, domain 2 Transl_elong_EFTu/EF1A_2 Domain
IPR005517 Translation elongation factor EFG/EF2, domain IV Transl_elong_EFG/EF2_IV Domain
IPR000795 Elongation factor, GTP-binding domain EF_GTP-bd_dom Domain
IPR014721 Ribosomal protein S5 domain 2-type fold, subgroup Ribosomal_S5_D2-typ_fold_subgr Domain

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Wintermeyer W Translational elongation factor G: a GTP-driven motor of the ribosome. 2000 Essays Biochem 35 117-29
Andersen GR Elongation factors in protein biosynthesis. 2003 Trends Biochem Sci 28 434-41
Nilsson J Elongation factors on the ribosome. 2005 Curr Opin Struct Biol 15 349-54
Andersen GR Structural studies of eukaryotic elongation factors. 2001 Cold Spring Harb Symp Quant Biol 66 425-37



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)