1cqz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:44, 7 February 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1cqz.jpg|left|200px]]<br /><applet load="1cqz" size="350" 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://oca.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://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:53 2008''
+

Current revision

CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE.

PDB ID 1cqz

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cqz"
Personal tools