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1d2e
From Proteopedia
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CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP
Overview
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 Structure
1D2E is a Single protein structure of sequence from Bos taurus with and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:12:15 2008
Categories: Bos taurus | Single protein | Andersen, G R. | Nyborg, J. | Spremulli, L L. | Thirup, S. | GDP | MG | Beta-barrel | G-protein
