2cjp

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[[Image:2cjp.gif|left|200px]]
 
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{{Structure
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==Structure of potato (Solanum tuberosum) epoxide hydrolase I (StEH1)==
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|PDB= 2cjp |SIZE=350|CAPTION= <scene name='initialview01'>2cjp</scene>, resolution 1.95&Aring;
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<StructureSection load='2cjp' size='340' side='right'caption='[[2cjp]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=VPR:2-PROPYLPENTANAMIDE'>VPR</scene>
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<table><tr><td colspan='2'>[[2cjp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CJP FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=VPR:2-PROPYLPENTANAMIDE'>VPR</scene></td></tr>
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|DOMAIN=
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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=2cjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjp OCA], [https://pdbe.org/2cjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cjp RCSB], [https://www.ebi.ac.uk/pdbsum/2cjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjp ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjp OCA], [http://www.ebi.ac.uk/pdbsum/2cjp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cjp RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q41415_SOLTU Q41415_SOLTU]
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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/cj/2cjp_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=2cjp ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Epoxide hydrolases catalyze the conversion of epoxides to diols. The known functions of such enzymes include detoxification of xenobiotics, drug metabolism, synthesis of signaling compounds, and intermediary metabolism. In plants, epoxide hydrolases are thought to participate in general defense systems. In the present study, we report the first structure of a plant epoxide hydrolase, one of the four homologous enzymes found in potato. The structure was solved by molecular replacement and refined to a resolution of 1.95 A. Analysis of the structure allows a better understanding of the observed substrate specificities and activity. Further, comparisons with mammalian and fungal epoxide hydrolase structures reported earlier show the basis of differing substrate specificities in the various epoxide hydrolase subfamilies. Most plant enzymes, like the potato epoxide hydrolase, are expected to be monomers with a preference for substrates with long lipid-like substituents of the epoxide ring. The significance of these results in the context of biological roles and industrial applications is discussed.
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'''STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I (STEH1)'''
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X-ray structure of potato epoxide hydrolase sheds light on substrate specificity in plant enzymes.,Mowbray SL, Elfstrom LT, Ahlgren KM, Andersson CE, Widersten M Protein Sci. 2006 Jul;15(7):1628-37. Epub 2006 Jun 2. PMID:16751602<ref>PMID:16751602</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2cjp" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Epoxide hydrolases catalyze the conversion of epoxides to diols. The known functions of such enzymes include detoxification of xenobiotics, drug metabolism, synthesis of signaling compounds, and intermediary metabolism. In plants, epoxide hydrolases are thought to participate in general defense systems. In the present study, we report the first structure of a plant epoxide hydrolase, one of the four homologous enzymes found in potato. The structure was solved by molecular replacement and refined to a resolution of 1.95 A. Analysis of the structure allows a better understanding of the observed substrate specificities and activity. Further, comparisons with mammalian and fungal epoxide hydrolase structures reported earlier show the basis of differing substrate specificities in the various epoxide hydrolase subfamilies. Most plant enzymes, like the potato epoxide hydrolase, are expected to be monomers with a preference for substrates with long lipid-like substituents of the epoxide ring. The significance of these results in the context of biological roles and industrial applications is discussed.
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*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2CJP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJP OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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X-ray structure of potato epoxide hydrolase sheds light on substrate specificity in plant enzymes., Mowbray SL, Elfstrom LT, Ahlgren KM, Andersson CE, Widersten M, Protein Sci. 2006 Jul;15(7):1628-37. Epub 2006 Jun 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16751602 16751602]
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[[Category: Microsomal epoxide hydrolase]]
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[[Category: Single protein]]
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[[Category: Solanum tuberosum]]
[[Category: Solanum tuberosum]]
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[[Category: Ahlgren, K M.]]
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[[Category: Ahlgren KM]]
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[[Category: Andersson, C E.]]
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[[Category: Andersson CE]]
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[[Category: Elfstrom, L T.]]
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[[Category: Elfstrom LT]]
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[[Category: Mowbray, S L.]]
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[[Category: Mowbray SL]]
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[[Category: Widersten, M.]]
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[[Category: Widersten M]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:22:28 2008''
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Current revision

Structure of potato (Solanum tuberosum) epoxide hydrolase I (StEH1)

PDB ID 2cjp

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