1cqz

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[[Image:1cqz.jpg|left|200px]]
[[Image:1cqz.jpg|left|200px]]
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{{Structure
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|PDB= 1cqz |SIZE=350|CAPTION= <scene name='initialview01'>1cqz</scene>, resolution 2.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1cqz", creates the "Structure Box" on the page.
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|SITE=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Microsomal_epoxide_hydrolase Microsomal epoxide hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 3.3.2.9] </span>
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{{STRUCTURE_1cqz| PDB=1cqz | SCENE= }}
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|RELATEDENTRY=[[1cr6|1CR6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqz OCA], [http://www.ebi.ac.uk/pdbsum/1cqz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cqz RCSB]</span>
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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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[[Category: alpha/beta hydrolase fold]]
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[[Category: Alpha/beta hydrolase fold]]
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[[Category: domain-swapping]]
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[[Category: Domain-swapping]]
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[[Category: homodimer]]
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[[Category: Homodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:26:58 2008''
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Revision as of 10:01, 2 May 2008

Template:STRUCTURE 1cqz

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

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