1d2e

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.