1nww

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[[Image:1nww.gif|left|200px]]
 
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==Limonene-1,2-epoxide hydrolase==
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The line below this paragraph, containing "STRUCTURE_1nww", creates the "Structure Box" on the page.
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<StructureSection load='1nww' size='340' side='right'caption='[[1nww]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1nww]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NWW FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HPN:HEPTANAMIDE'>HPN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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{{STRUCTURE_1nww| PDB=1nww | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nww OCA], [https://pdbe.org/1nww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nww RCSB], [https://www.ebi.ac.uk/pdbsum/1nww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nww ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIMA_RHOER LIMA_RHOER] Catalyzes the conversion of limonene-1,2-epoxide to limonene-1,2-diol. Can use both the (-) and (+) isomers of limonene-1,2-epoxide as substrates and also has some activity with 1-methylcyclohexene oxide, cyclohexene oxide and indene oxide as substrates.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nw/1nww_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1nww ConSurf].
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<div style="clear:both"></div>
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'''Limonene-1,2-epoxide hydrolase'''
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==See Also==
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*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a deep pocket. Although most residues lining this pocket are hydrophobic, a cluster of polar groups, including an Asp-Arg-Asp triad, interact at its deepest point. Site-directed mutagenesis supports the conclusion that this is the active site. Further, a 1.7 A resolution structure shows the inhibitor valpromide bound at this position, with its polar atoms interacting directly with the residues of the triad. We suggest that several bacterial proteins of currently unknown function will share this structure and, in some cases, catalytic properties.
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[[Category: Large Structures]]
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==About this Structure==
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1NWW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWW OCA].
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==Reference==
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Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site., Arand M, Hallberg BM, Zou J, Bergfors T, Oesch F, van der Werf MJ, de Bont JA, Jones TA, Mowbray SL, EMBO J. 2003 Jun 2;22(11):2583-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12773375 12773375]
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[[Category: Limonene-1,2-epoxide hydrolase]]
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[[Category: Rhodococcus erythropolis]]
[[Category: Rhodococcus erythropolis]]
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[[Category: Single protein]]
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[[Category: Arand M]]
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[[Category: Arand, M.]]
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[[Category: Bergfors T]]
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[[Category: Bergfors, T.]]
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[[Category: Hallberg BM]]
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[[Category: Bont, J A.M de.]]
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[[Category: Jones TA]]
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[[Category: Hallberg, B M.]]
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[[Category: Mowbray SL]]
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[[Category: Jones, T A.]]
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[[Category: Oesch F]]
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[[Category: Mowbray, S L.]]
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[[Category: Zou J]]
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[[Category: Oesch, F.]]
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[[Category: De Bont JAM]]
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[[Category: Werf, M J.van der.]]
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[[Category: Van der Werf MJ]]
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[[Category: Zou, J.]]
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[[Category: Epoxide hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:04:39 2008''
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Current revision

Limonene-1,2-epoxide hydrolase

PDB ID 1nww

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