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| | ==Crystal structure of yeast enoyl-CoA isomerase helix-10 deletion (ScECI2-H10) mutant== | | ==Crystal structure of yeast enoyl-CoA isomerase helix-10 deletion (ScECI2-H10) mutant== |
| - | <StructureSection load='4zdf' size='340' side='right' caption='[[4zdf]], [[Resolution|resolution]] 1.81Å' scene=''> | + | <StructureSection load='4zdf' size='340' side='right'caption='[[4zdf]], [[Resolution|resolution]] 1.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zdf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZDF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zdf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZDF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdf OCA], [https://pdbe.org/4zdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zdf RCSB], [https://www.ebi.ac.uk/pdbsum/4zdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdf ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECI1, YLR284C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdf OCA], [http://pdbe.org/4zdf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zdf RCSB], [http://www.ebi.ac.uk/pdbsum/4zdf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ECI1_YEAST ECI1_YEAST]] Essential for the beta oxidation of unsaturated fatty acids.<ref>PMID:9837886</ref> | + | [https://www.uniprot.org/uniprot/ECI1_YEAST ECI1_YEAST] Essential for the beta oxidation of unsaturated fatty acids.<ref>PMID:9837886</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Dodecenoyl-CoA isomerase]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Koski, M K]] | + | [[Category: Koski MK]] |
| - | [[Category: Onwukwe, G U]] | + | [[Category: Onwukwe GU]] |
| - | [[Category: Wierenga, R K]] | + | [[Category: Wierenga RK]] |
| - | [[Category: Beta-oxidation]]
| + | |
| - | [[Category: Crotonase]]
| + | |
| - | [[Category: Enoyl-coa isomerase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Function
ECI1_YEAST Essential for the beta oxidation of unsaturated fatty acids.[1]
Publication Abstract from PubMed
Delta(3),Delta(2)-Enoyl-CoA isomerases (ECIs) catalyze the shift of a double bond from 3Z- or 3E-enoyl-CoA to 2E-enoyl-CoA. ECIs are members of the crotonase superfamily. The crotonase framework is used by many enzymes to catalyze a wide range of reactions on acyl-CoA thioesters. The thioester O atom is bound in a conserved oxyanion hole. Here, the mode of binding of acyl-CoA substrate analogues to peroxisomal Saccharomyces cerevisiae ECI (ScECI2) is described. The best defined part of the bound acyl-CoA molecules is the 3',5'-diphosphate-adenosine moiety, which interacts with residues of loop 1 and loop 2, whereas the pantetheine part is the least well defined. The catalytic base, Glu158, is hydrogen-bonded to the Asn101 side chain and is further hydrogen-bonded to the side chain of Arg100 in the apo structure. Arg100 is completely buried in the apo structure and a conformational change of the Arg100 side chain appears to be important for substrate binding and catalysis. The oxyanion hole is formed by the NH groups of Ala70 (loop 2) and Leu126 (helix 3). The O atoms of the corresponding peptide units, Gly69 O and Gly125 O, are both part of extensive hydrogen-bond networks. These hydrogen-bond networks are a conserved feature of the crotonase oxyanion hole and their importance for catalysis is discussed.
Structures of yeast peroxisomal Delta(3),Delta(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole.,Onwukwe GU, Koski MK, Pihko P, Schmitz W, Wierenga RK Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2178-91. doi:, 10.1107/S139900471501559X. Epub 2015 Oct 27. PMID:26527136[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Geisbrecht BV, Zhu D, Schulz K, Nau K, Morrell JC, Geraghty M, Schulz H, Erdmann R, Gould SJ. Molecular characterization of Saccharomyces cerevisiae Delta3, Delta2-enoyl-CoA isomerase. J Biol Chem. 1998 Dec 11;273(50):33184-91. PMID:9837886
- ↑ Onwukwe GU, Koski MK, Pihko P, Schmitz W, Wierenga RK. Structures of yeast peroxisomal Delta(3),Delta(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole. Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2178-91. doi:, 10.1107/S139900471501559X. Epub 2015 Oct 27. PMID:26527136 doi:http://dx.doi.org/10.1107/S139900471501559X
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