1ehy
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(New page: 200px<br /><applet load="1ehy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ehy, resolution 2.1Å" /> '''X-ray structure of th...)
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Revision as of 20:10, 24 November 2007
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X-ray structure of the epoxide hydrolase from agrobacterium radiobacter ad1
Overview
Epoxide hydrolases catalyze the cofactor-independent hydrolysis of, reactive and toxic epoxides. They play an essential role in the, detoxification of various xenobiotics in higher organisms and in the, bacterial degradation of several environmental pollutants. The first x-ray, structure of one of these, from Agrobacterium radiobacter AD1, has been, determined by isomorphous replacement at 2.1-A resolution. The enzyme, shows a two-domain structure with the core having the alpha/beta, hydrolase-fold topology. The catalytic residues, Asp107 and His275, are, located in a predominantly hydrophobic environment between the two, domains. A tunnel connects the back of the active-site cavity with the, surface of the enzyme and provides access to the active site for the, catalytic water molecule, which in the crystal structure, has been found, at hydrogen bond distance to His275. Because of a crystallographic, contact, the active site has become accessible for the Gln134 side chain, which occupies a position mimicking a bound substrate. The structure, suggests Tyr152/Tyr215 as the residues involved in substrate binding, stabilization of the transition state, and possibly protonation of the, epoxide oxygen.
About this Structure
1EHY is a Single protein structure of sequence from Agrobacterium tumefaciens with K as ligand. Active as Microsomal epoxide hydrolase, with EC number 3.3.2.9 Full crystallographic information is available from OCA.
Reference
The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1. An enzyme to detoxify harmful epoxides., Nardini M, Ridder IS, Rozeboom HJ, Kalk KH, Rink R, Janssen DB, Dijkstra BW, J Biol Chem. 1999 May 21;274(21):14579-86. PMID:10329649
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