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1cqz
From Proteopedia
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[[Image:1cqz.jpg|left|200px]] | [[Image:1cqz.jpg|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE.''' | '''CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE.''' | ||
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[[Category: Hammock, B D.]] | [[Category: Hammock, B D.]] | ||
[[Category: Morisseau, C.]] | [[Category: Morisseau, C.]] | ||
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Revision as of 10:01, 2 May 2008
CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE.
Overview
The crystal structure of recombinant murine liver cytosolic epoxide hydrolase (EC 3.3.2.3) has been determined at 2.8-A resolution. The binding of a nanomolar affinity inhibitor confirms the active site location in the C-terminal domain; this domain is similar to that of haloalkane dehalogenase and shares the alpha/beta hydrolase fold. A structure-based mechanism is proposed that illuminates the unique chemical strategy for the activation of endogenous and man-made epoxide substrates for hydrolysis and detoxification. Surprisingly, a vestigial active site is found in the N-terminal domain similar to that of another enzyme of halocarbon metabolism, haloacid dehalogenase. Although the vestigial active site does not participate in epoxide hydrolysis, the vestigial domain plays a critical structural role by stabilizing the dimer in a distinctive domain-swapped architecture. Given the genetic and structural relationships among these enzymes of xenobiotic metabolism, a structure-based evolutionary sequence is postulated.
About this Structure
1CQZ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase., Argiriadi MA, Morisseau C, Hammock BD, Christianson DW, Proc Natl Acad Sci U S A. 1999 Sep 14;96(19):10637-42. PMID:10485878 Page seeded by OCA on Fri May 2 13:01:28 2008
