EFG_CElongation factor G C-terminus
|SMART accession number:||SM00838|
|Description:||This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.|
|Interpro abstract (IPR000640):|
Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [(PUBMED:12762045), (PUBMED:15922593), (PUBMED:12932732)]. 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.
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 [(PUBMED:12762009), (PUBMED:12762047)]. 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.
This entry represents the C-terminal domain found in EF2 (or EF-G) of both prokaryotes and eukaryotes (also known as eEF2), as well as in some tetracycline-resistance proteins. This domain 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, with which it forms the C-terminal block, but these two domains cannot be superimposed [(PUBMED:12471894)]. This domain is often found associated with (IPR000795), which contains the signatures for the N terminus of the proteins.
More information about these proteins can be found at Protein of the Month: Elongation Factors .
|GO function:||GTP binding (GO:0005525)|
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- Evolution (species in which this domain is found)
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- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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