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New page: left|200px<br /><applet load="1cqz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cqz, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1cqz.jpg|left|200px]]<br /><applet load="1cqz" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cqz, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE.'''<br />


==Overview==
==CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE.==
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.
<StructureSection load='1cqz' size='340' side='right'caption='[[1cqz]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cqz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CQZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqz OCA], [https://pdbe.org/1cqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cqz RCSB], [https://www.ebi.ac.uk/pdbsum/1cqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cqz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HYES_MOUSE HYES_MOUSE] Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cq/1cqz_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cqz ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CQZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CQZ OCA].
*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10485878 10485878]
[[Category: Large Structures]]
[[Category: Microsomal epoxide hydrolase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Argiriadi MA]]
[[Category: Argiriadi, M.A.]]
[[Category: Christianson DW]]
[[Category: Christianson, D.W.]]
[[Category: Hammock BD]]
[[Category: Hammock, B.D.]]
[[Category: Morisseau C]]
[[Category: Morisseau, C.]]
[[Category: alpha/beta hydrolase fold]]
[[Category: domain-swapping]]
[[Category: homodimer]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:41:22 2007''

Latest revision as of 06:44, 7 February 2024

CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE.

1cqz, resolution 2.80Å

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