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| | ==Crystal structure of acyl-coA oxidase3 from Yarrowia lipolytica== | | ==Crystal structure of acyl-coA oxidase3 from Yarrowia lipolytica== |
| - | <StructureSection load='5ys9' size='340' side='right' caption='[[5ys9]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='5ys9' size='340' side='right'caption='[[5ys9]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ys9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_lipolytica Candida lipolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YS9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YS9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ys9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yarrowia_lipolytica_CLIB122 Yarrowia lipolytica CLIB122]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YS9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YS9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">POX3, ACO3, YALI0D24750g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284591 Candida lipolytica])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-CoA_oxidase Acyl-CoA oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.6 1.3.3.6] </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=5ys9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ys9 OCA], [https://pdbe.org/5ys9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ys9 RCSB], [https://www.ebi.ac.uk/pdbsum/5ys9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ys9 ProSAT]</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=5ys9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ys9 OCA], [http://pdbe.org/5ys9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ys9 RCSB], [http://www.ebi.ac.uk/pdbsum/5ys9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ys9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACOX3_YARLI ACOX3_YARLI]] Oxidizes aliphatic acyl-CoA substrates of different chain lengths such as hexanoyl-CoA, decanoyl-CoA and myristyl-CoA as well as aromatic/heterocyclic ring-substituted chromogenic substrates, such as furylpropionyl-CoA. Of the above substrates, the efficiency of the enzyme, exhibits the following order: decanoyl-CoA > myristyl-CoA > hexanoyl-CoA > furyl-propionyl-CoA. | + | [https://www.uniprot.org/uniprot/ACOX3_YARLI ACOX3_YARLI] Oxidizes aliphatic acyl-CoA substrates of different chain lengths such as hexanoyl-CoA, decanoyl-CoA and myristyl-CoA as well as aromatic/heterocyclic ring-substituted chromogenic substrates, such as furylpropionyl-CoA. Of the above substrates, the efficiency of the enzyme, exhibits the following order: decanoyl-CoA > myristyl-CoA > hexanoyl-CoA > furyl-propionyl-CoA. |
| | <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: Acyl-CoA oxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Candida lipolytica]] | + | [[Category: Yarrowia lipolytica CLIB122]] |
| - | [[Category: Kim, K J]] | + | [[Category: Kim K-J]] |
| - | [[Category: Kim, S]] | + | [[Category: Kim S]] |
| - | [[Category: Fad-binding protein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
ACOX3_YARLI Oxidizes aliphatic acyl-CoA substrates of different chain lengths such as hexanoyl-CoA, decanoyl-CoA and myristyl-CoA as well as aromatic/heterocyclic ring-substituted chromogenic substrates, such as furylpropionyl-CoA. Of the above substrates, the efficiency of the enzyme, exhibits the following order: decanoyl-CoA > myristyl-CoA > hexanoyl-CoA > furyl-propionyl-CoA.
Publication Abstract from PubMed
Acyl-CoA oxidases (ACOXs) play important roles in lipid metabolism, including peroxisomal fatty acid beta-oxidation by the conversion of acyl-CoAs to 2-trans-enoyl-CoAs. The yeast Yarrowia lipolyticacan utilize fatty acidsas a carbon source and thus has extensive biotechnological applications. The crystal structure of ACOX3from Y. lipolytica(YlACOX3) was determinedat a resolution of2.5 A. It contained two molecules per asymmetric unit, and the monomeric structure was folded into four domains, Nalpha, Nbeta, Calpha1 and Calpha2domains. The cofactor flavin adenine dinucleotide (FAD)was bound in the dimer interface. The substrate-binding pocket was located near the cofactor and formed at the interface between the Nalpha, Nbeta, and Calpha1 domains. Comparisons with the other ACOX structures provided structural insights into how YlACOX has a substrate preference for short-chain acyl-CoA. In addition, the structure of YlACOX3 was compared to those of medium- and long-chain ACOXs, and the structural basis for their differences in substrate specificity was discussed.
Crystal structure of acyl-CoA oxidase3from Yarrowia lipolyticawith specificity for short-chain acyl-CoA.,Kim S, Kim KJ J Microbiol Biotechnol. 2018 Feb 13. pii: 10.4014/jmb.1711.11032. doi:, 10.4014/jmb.1711.11032. PMID:29429324[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim S, Kim KJ. Crystal structure of acyl-CoA oxidase3from Yarrowia lipolyticawith specificity for short-chain acyl-CoA. J Microbiol Biotechnol. 2018 Feb 13. pii: 10.4014/jmb.1711.11032. doi:, 10.4014/jmb.1711.11032. PMID:29429324 doi:http://dx.doi.org/10.4014/jmb.1711.11032
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