1d2e
From Proteopedia
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|PDB= 1d2e |SIZE=350|CAPTION= <scene name='initialview01'>1d2e</scene>, resolution 1.94Å | |PDB= 1d2e |SIZE=350|CAPTION= <scene name='initialview01'>1d2e</scene>, resolution 1.94Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1efc|1EFC]], [[1tui|1TUI]] | ||
| + | |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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[[Category: Spremulli, L L.]] | [[Category: Spremulli, L L.]] | ||
[[Category: Thirup, S.]] | [[Category: Thirup, S.]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
[[Category: g-protein]] | [[Category: g-protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:33:16 2008'' |
Revision as of 16:33, 30 March 2008
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| , resolution 1.94Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1EFC, 1TUI
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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