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1oix

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[[Image:1oix.gif|left|200px]]
[[Image:1oix.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1oix", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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{{STRUCTURE_1oix| PDB=1oix | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oix OCA], [http://www.ebi.ac.uk/pdbsum/1oix PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oix RCSB]</span>
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'''X-RAY STRUCTURE OF THE SMALL G PROTEIN RAB11A IN COMPLEX WITH GDP AND PI'''
'''X-RAY STRUCTURE OF THE SMALL G PROTEIN RAB11A IN COMPLEX WITH GDP AND PI'''
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[[Category: Salamero, J.]]
[[Category: Salamero, J.]]
[[Category: Senic-Matuglia, F.]]
[[Category: Senic-Matuglia, F.]]
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[[Category: gtp-binding]]
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[[Category: Gtp-binding]]
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[[Category: intracellular trafficking]]
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[[Category: Intracellular trafficking]]
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[[Category: lipoprotein]]
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[[Category: Lipoprotein]]
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[[Category: prenylation]]
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[[Category: Prenylation]]
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[[Category: protein transport]]
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[[Category: Protein transport]]
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[[Category: small g protein]]
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[[Category: Small g protein]]
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Revision as of 00:54, 3 May 2008

Template:STRUCTURE 1oix

X-RAY STRUCTURE OF THE SMALL G PROTEIN RAB11A IN COMPLEX WITH GDP AND PI


Overview

GTP hydrolysis by small GTP binding proteins of the Ras superfamily is a universal reaction that controls multiple cellular regulations. Its enzymic mechanism has been the subject of long-standing debates as to the existence/identity of the general base and the electronic nature of its transition state. Here we report the high-resolution crystal structure of a small GTP binding protein, Rab11, solved in complex with GDP and Pi. Unexpectedly, a Pi oxygen and the GDP-cleaved oxygen are located less than 2.5 A apart, suggesting that they share a proton, likely in the form of a low-barrier hydrogen bond. This implies that the gamma-phosphate of GTP was protonated; hence, that GTP acts as a general base. Furthermore, this interaction should establish at, and stabilize, the transition state. Altogether, we propose a revised model for the GTPase reaction that should reconcile earlier models into a unique substrate-assisted mechanism.

About this Structure

1OIX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystallographic evidence for substrate-assisted GTP hydrolysis by a small GTP binding protein., Pasqualato S, Cherfils J, Structure. 2005 Apr;13(4):533-40. PMID:15837192 Page seeded by OCA on Sat May 3 03:54:24 2008

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