1cr6: Difference between revisions

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-[[Image:1cr6.gif|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH CPU INHIBITOR==
-The line below this paragraph, containing "STRUCTURE_1cr6", creates the "Structure Box" on the page.
+<StructureSection load='1cr6' size='340' side='right'caption='[[1cr6]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1cr6]] 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=1CR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CR6 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPU:N-CYCLOHEXYL-N-(PROPYL)PHENYL+UREA'>CPU</scene></td></tr>
-{{STRUCTURE_1cr6|  PDB=1cr6  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cr6 OCA], [https://pdbe.org/1cr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cr6 RCSB], [https://www.ebi.ac.uk/pdbsum/1cr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cr6 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/cr/1cr6_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=1cr6 ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH CPU INHIBITOR'''
+==See Also==
+*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
-==About this Structure==
-CR6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CR6 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:[http://www.ncbi.nlm.nih.gov/pubmed/10485878 10485878]
-[[Category: Microsomal epoxide hydrolase]]
 [[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: Disubstituted urea inhibitor]]
-[[Category: Homodimer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:02:00 2008''