1dci

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(New page: 200px<br /> <applet load="1dci" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dci, resolution 1.5&Aring;" /> '''DIENOYL-COA ISOMERAS...)
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[[Image:1dci.gif|left|200px]]<br />
 
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<applet load="1dci" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dci, resolution 1.5&Aring;" />
 
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'''DIENOYL-COA ISOMERASE'''<br />
 
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==Overview==
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==DIENOYL-COA ISOMERASE==
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BACKGROUND: The degradation of unsaturated fatty acids is vital to all, living organisms. Certain unsaturated fatty acids must be catabolized via, a pathway auxiliary to the main beta-oxidation pathway. Dienoyl-coenzyme A, (dienoyl-CoA) isomerase catalyzes one step of this auxiliary pathway, the, isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA, and is imported into both mitochondria and peroxisomes. Dienoyl-CoA, isomerase belongs to a family of CoA-binding proteins that share the, enoyl-CoA hydratase/isomerase sequence motif. RESULTS: The crystal, structure of rat dienoyl-CoA isomerase has been determined at 1.5 A, resolution. The fold closely resembles that of enoyl-CoA hydratase and, 4-chlorobenzoyl-CoA dehalogenase. Dienoyl-CoA isomerase forms hexamers, made ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9739087 (full description)]]
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<StructureSection load='1dci' size='340' side='right'caption='[[1dci]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1dci]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCI FirstGlance]. <br>
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1DCI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with SO4, MG and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DCI OCA]].
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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]] 1.5&#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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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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=1dci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dci OCA], [https://pdbe.org/1dci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dci RCSB], [https://www.ebi.ac.uk/pdbsum/1dci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dci ProSAT]</span></td></tr>
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The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis., Modis Y, Filppula SA, Novikov DK, Norledge B, Hiltunen JK, Wierenga RK, Structure. 1998 Aug 15;6(8):957-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9739087 9739087]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ECH1_RAT ECH1_RAT] Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.
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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/dc/1dci_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=1dci ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Filppula SA]]
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[[Category: Filppula, S.A.]]
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[[Category: Hiltunen JK]]
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[[Category: Hiltunen, J.K.]]
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[[Category: Modis Y]]
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[[Category: Modis, Y.]]
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[[Category: Norledge B]]
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[[Category: Norledge, B.]]
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[[Category: Novikov D]]
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[[Category: Novikov, D.]]
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[[Category: Wierenga RK]]
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[[Category: Wierenga, R.K.]]
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[[Category: EDO]]
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[[Category: MG]]
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[[Category: SO4]]
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[[Category: dienoyl-coa isomerase]]
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[[Category: lyase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:56:32 2007''
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Current revision

DIENOYL-COA ISOMERASE

PDB ID 1dci

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