Structural highlights
Function
[EFTU_BOVIN] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of bovine mitochondrial elongation factor Tu (EF-Tu) in complex with GDP has been determined at a resolution of 1. 94 A. The structure is similar to that of EF-Tu:GDP from Escherichia coli and Thermus aquaticus, but the orientation of the GDP-binding domain 1 is changed relative to domains 2 and 3. Sixteen conserved water molecules common to EF-Tu and other G-proteins in the GDP-binding site are described. These water molecules create a network linking separated parts of the binding pocket. Mitochondrial EF-Tu binds nucleotides less tightly than prokaryotic EF-Tu possibly due to an increased mobility in regions close to the GDP-binding site. The C-terminal extension of mitochondrial EF-Tu has structural similarities with DNA recognising zinc fingers suggesting that the extension may be involved in recognition of RNA.
High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP.,Andersen GR, Thirup S, Spremulli LL, Nyborg J J Mol Biol. 2000 Mar 24;297(2):421-36. PMID:10715211[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Andersen GR, Thirup S, Spremulli LL, Nyborg J. High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP. J Mol Biol. 2000 Mar 24;297(2):421-36. PMID:10715211 doi:10.1006/jmbi.2000.3564
