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1sg4

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(New page: 200px<br /> <applet load="1sg4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sg4, resolution 1.30&Aring;" /> '''Crystal structure o...)
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[[Image:1sg4.gif|left|200px]]<br />
 
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<applet load="1sg4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sg4, resolution 1.30&Aring;" />
 
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'''Crystal structure of human mitochondrial delta3-delta2-enoyl-CoA isomerase'''<br />
 
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==Overview==
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==Crystal structure of human mitochondrial delta3-delta2-enoyl-CoA isomerase==
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The crystal structure of Delta3-Delta2-enoyl-CoA isomerase from human, mitochondria (hmEci), complexed with the substrate analogue octanoyl-CoA, has been refined at 1.3 A resolution. This enzyme takes part in the, beta-oxidation of unsaturated fatty acids by converting both cis-3 and, trans-3-enoyl-CoA esters (with variable length of the acyl group) to, trans-2-enoyl-CoA. hmEci belongs to the hydratase/isomerase (crotonase), superfamily. Most of the enzymes belonging to this superfamily are, hexamers, but hmEci is shown to be a trimer. The mode of binding of the, ligand, octanoyl-CoA, shows that the omega-end of the acyl group binds in, a hydrophobic tunnel formed by residues of the loop preceding helix H4 as, well as by side-chains of the kinked helix H9. From the structure of the, complex it can be seen that Glu136 is the only catalytic residue. The, importance of Glu136 for catalysis is confirmed by mutagenesis studies. A, cavity analysis shows the presence of two large, adjacent empty, hydrophobic cavities near the active site, which are shaped by side-chains, of helices H1, H2, H3 and H4. The structure comparison of hmEci with, structures of other superfamily members, in particular of rat, mitochondrial hydratase (crotonase) and yeast peroxisomal enoyl-CoA, isomerase, highlights the variable mode of binding of the fatty acid, moiety in this superfamily.
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<StructureSection load='1sg4' size='340' side='right'caption='[[1sg4]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1sg4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SG4 FirstGlance]. <br>
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1SG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CO8 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dodecenoyl-CoA_isomerase Dodecenoyl-CoA isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.8 5.3.3.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SG4 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]] 1.3&#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=CO8:OCTANOYL-COENZYME+A'>CO8</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=1sg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sg4 OCA], [https://pdbe.org/1sg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sg4 RCSB], [https://www.ebi.ac.uk/pdbsum/1sg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sg4 ProSAT]</span></td></tr>
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The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group., Partanen ST, Novikov DK, Popov AN, Mursula AM, Hiltunen JK, Wierenga RK, J Mol Biol. 2004 Sep 24;342(4):1197-208. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15351645 15351645]
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</table>
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[[Category: Dodecenoyl-CoA isomerase]]
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== Function ==
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[https://www.uniprot.org/uniprot/ECI1_HUMAN ECI1_HUMAN] Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species.
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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/sg/1sg4_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=1sg4 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hiltunen, J.K.]]
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[[Category: Hiltunen JK]]
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[[Category: Mursula, A.M.]]
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[[Category: Mursula AM]]
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[[Category: Novikov, D.K.]]
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[[Category: Novikov DK]]
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[[Category: Partanen, S.T.]]
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[[Category: Partanen ST]]
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[[Category: Popov, A.N.]]
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[[Category: Popov AN]]
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[[Category: Wierenga, R.K.]]
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[[Category: Wierenga RK]]
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[[Category: CO8]]
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[[Category: crotonase fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:13:13 2007''
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Current revision

Crystal structure of human mitochondrial delta3-delta2-enoyl-CoA isomerase

PDB ID 1sg4

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