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1oix

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: small g protein]]
[[Category: small g protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:58:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:18 2008''

Revision as of 12:18, 21 February 2008

Image:1oix.gif

1oix, resolution 1.7Å

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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 with , , and as ligands. Known structural/functional Site: . 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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