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| | <StructureSection load='1pjh' size='340' side='right'caption='[[1pjh]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1pjh' size='340' side='right'caption='[[1pjh]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pjh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PJH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pjh]] is a 3 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=1PJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PJH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hno|1hno]], [[1hnu|1hnu]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECI1 ([https://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'>[https://en.wikipedia.org/wiki/Dodecenoyl-CoA_isomerase Dodecenoyl-CoA isomerase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=1pjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pjh OCA], [https://pdbe.org/1pjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pjh RCSB], [https://www.ebi.ac.uk/pdbsum/1pjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pjh ProSAT]</span></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=1pjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pjh OCA], [https://pdbe.org/1pjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pjh RCSB], [https://www.ebi.ac.uk/pdbsum/1pjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pjh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| - | [[Category: Dodecenoyl-CoA isomerase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hiltunen, J K]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Mursula, A M]] | + | [[Category: Hiltunen JK]] |
| - | [[Category: Wierenga, R K]] | + | [[Category: Mursula AM]] |
| - | [[Category: Beta-beta-alpha spiral fold]] | + | [[Category: Wierenga RK]] |
| - | [[Category: Inter-trimer contact]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Function
ECI1_YEAST Essential for the beta oxidation of unsaturated fatty acids.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Subunits of the enzymes in the crotonase superfamily form tight trimeric disks. In most members of this protein superfamily these disks assemble further into hexamers. Here we report on the 2.1 A structure of a tight hexameric crystal form of the yeast peroxisomal delta(3)-delta(2)-enoyl-CoA isomerase (Eci1p). A comparison of this structure to a previously solved crystal form of Eci1p and other structures of this superfamily shows that there is much variability with respect to the relative distance between the disks and their relative orientations. In particular helices H2 and H9 are involved in the inter-trimer contacts and there are considerable structural differences in these helices in this superfamily. Helices H2 and H9 are near the catalytic cavity and it is postulated that the observed structural variability of these helices, stabilized by the different modes of assembly, has allowed the evolution of the wide range of substrate and catalytic specificity within this enzyme superfamily.
Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily.,Mursula AM, Hiltunen JK, Wierenga RK FEBS Lett. 2004 Jan 16;557(1-3):81-7. PMID:14741345[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
- ↑ Mursula AM, Hiltunen JK, Wierenga RK. Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily. FEBS Lett. 2004 Jan 16;557(1-3):81-7. PMID:14741345
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