1oix
From Proteopedia
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|PDB= 1oix |SIZE=350|CAPTION= <scene name='initialview01'>1oix</scene>, resolution 1.7Å | |PDB= 1oix |SIZE=350|CAPTION= <scene name='initialview01'>1oix</scene>, resolution 1.7Å | ||
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Salamero, J.]] | [[Category: Salamero, J.]] | ||
[[Category: Senic-Matuglia, F.]] | [[Category: Senic-Matuglia, F.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PO4]] | ||
[[Category: gtp-binding]] | [[Category: gtp-binding]] | ||
[[Category: intracellular trafficking]] | [[Category: intracellular trafficking]] | ||
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[[Category: small g protein]] | [[Category: small 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 22:45:59 2008'' |
Revision as of 19:46, 30 March 2008
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| , resolution 1.7Å | |||||||
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| Sites: | |||||||
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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