InterPro domain: IPR009001

A beta barrel of circularly permuted topology is found in the C terminus of many translation elongation and initiation factors. This domain is found in the elongation factors EF1A (or EF-Tu) of both eukaryotes and prokaryotes, which functions to recognise and transport aminoacyl-tRNA to the acceptor (A) site of the ribosome during the elongation process [ 1 , 2 ]. This domain is also found in the initiation factor IF2 gamma subunit of eukaryotes [ 3 ], which functions to transport the initiator methionyl-tRNA to the ribosome. The C-terminal extension of mitochondrial EF1A (or EF-Tu) has structural similarities with DNA recognising zinc fingers, suggesting that the extension may be involved in recognition of RNA.

1. High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP. J. Mol. Biol. 297, 421-36
2. Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. Mol. Cell 6, 1261-6
3. The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J. 21, 1821-32