1d2e
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CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP
OverviewOverview
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.
About this StructureAbout this Structure
1D2E is a Single protein structure of sequence from Bos taurus with MG and GDP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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