1d2e

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[[Image:1d2e.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_1d2e| PDB=1d2e | SCENE= }}
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|RELATEDENTRY=[[1efc|1EFC]], [[1tui|1TUI]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d2e OCA], [http://www.ebi.ac.uk/pdbsum/1d2e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d2e RCSB]</span>
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'''CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP'''
'''CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP'''
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[[Category: Spremulli, L L.]]
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[[Category: Thirup, S.]]
[[Category: Thirup, S.]]
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[[Category: Beta-barrel]]
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[[Category: g-protein]]
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Revision as of 10:22, 2 May 2008

Template:STRUCTURE 1d2e

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. 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 Fri May 2 13:22:19 2008

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