InterPro : IPR004160

Name  Translation elongation factor EFTu/EF1A, C-terminal Short Name  Transl_elong_EFTu/EF1A_C
Type  Domain 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, therebyfreeing 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.EF1A (also known as EF-1alpha or EF-Tu) is a G-protein. It forms a ternary complex of EF1A-GTP-aminoacyltRNA. The binding of aminoacyl-tRNA stimulates GTP hydrolysis by EF1A, causing a conformational change in EF1A that causes EF1A-GDP to detach from the ribosome, leaving the aminoacyl-tRNA attached at the A-site. Only the cognate aminoacyl-tRNA can induce the required conformational change in EF1A through its tight anticodon-codon binding [, ]. EF1A-GDP is returned to its active state, EF1A-GTP, through the action of another elongation factor, EF1B (also known as EF-Ts or EF-1beta/gamma/delta).EF1A consists of three structural domains. This entry represents the C-terminal domain, which adopts a beta-barrel structure, and is involved in binding to both charged tRNA and to EF1B (or EF-Ts, ) [].
 Feedback

Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

3 Found In

Id Name Short Name Type
IPR004539 Translation elongation factor EF1A, eukaryotic/archaeal Transl_elong_EF1A_euk/arc Family
IPR004541 Translation elongation factor EFTu/EF1A, bacterial/organelle Transl_elong_EFTu/EF1A_bac/org Family
IPR003285 Yeast eukaryotic release factor Yeast_ERF Family

1 Parent Features

Id Name Short Name Type
IPR009001 Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal Transl_elong_EF1A/Init_IF2_C Domain

6 Publications

First Author Title Year Journal Volume Pages
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
Wang Y Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus. 1997 Nat Struct Biol 4 650-6
Rodnina MV Recognition and selection of tRNA in translation. 2005 FEBS Lett 579 938-42
Krab IM Mechanisms of EF-Tu, a pioneer GTPase. 2002 Prog Nucleic Acid Res Mol Biol 71 513-51



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)