InterPro : IPR000640

Name  Translation elongation factor EFG, V domain Short Name  EFG_V
Type  Domain Description  Elongation factor EF2 (EF-G) is a G-protein. It brings about the translocation of peptidyl-tRNA and mRNA through a ratchet-like mechanism: the binding of GTP-EF2 to the ribosome causes a counter-clockwise rotation in the small ribosomal subunit; the hydrolysis of GTP to GDP by EF2 and the subsequent release of EF2 causes a clockwise rotation of the small subunit back to the starting position [, ]. This twisting action destabilises tRNA-ribosome interactions, freeing the tRNA to translocate along the ribosome upon GTP-hydrolysis by EF2. EF2 binding also affects the entry and exit channel openings for the mRNA, widening it when bound to enable the mRNA to translocate along the ribosome.EF2 is folded into five domains, with domains I and II forming the N-terminal block, domains IV and V forming the C-terminal block, and domain III providing the covalently-linked flexible connection between the two []. This entry represents the domain V of EF2 of both prokaryotes and eukaryotes (also known as eEF2). This domain is also found in some tetracycline-resistance proteins. It adopts a ferredoxin-like fold consisting of an alpha/beta sandwich with anti-parallel beta-sheets. It resembles the topology of domain III found in these elongation factors, but these two domains cannot be superimposed [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

4 Found In

Id Name Short Name Type
IPR004540 Translation elongation factor EFG/EF2 Transl_elong_EFG/EF2 Family
IPR006298 GTP-binding protein TypA TypA_GTP-bd Family
IPR004543 Translation elongation factor EFG/EF2, archaeal Transl_elong_EFG/EF2_arc Family
IPR006297 Elongation factor 4 EF-4 Family

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Laurberg M Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. 2000 J Mol Biol 303 593-603
Wintermeyer W Translational elongation factor G: a GTP-driven motor of the ribosome. 2000 Essays Biochem 35 117-29
Frank J Ratchet-like movements between the two ribosomal subunits: their implications in elongation factor recognition and tRNA translocation. 2001 Cold Spring Harb Symp Quant Biol 66 67-75
Wintermeyer W Mechanism of elongation factor G function in tRNA translocation on the ribosome. 2001 Cold Spring Harb Symp Quant Biol 66 449-58



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)