5k3h: Difference between revisions

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<StructureSection load='5k3h' size='340' side='right'caption='[[5k3h]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
<StructureSection load='5k3h' size='340' side='right'caption='[[5k3h]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5k3h]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K3H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K3H FirstGlance]. <br>
<table><tr><td colspan='2'>[[5k3h]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K3H FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k3g|5k3g]], [[5k3i|5k3i]], [[5k3j|5k3j]]</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]] 2.48&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acox-1, CELE_F08A8.1, F08A8.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=5k3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k3h OCA], [https://pdbe.org/5k3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k3h RCSB], [https://www.ebi.ac.uk/pdbsum/5k3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k3h 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=5k3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k3h OCA], [http://pdbe.org/5k3h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k3h RCSB], [http://www.ebi.ac.uk/pdbsum/5k3h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k3h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACX11_CAEEL ACX11_CAEEL] Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains (PubMed:25775534, PubMed:29537254, PubMed:27551084). Specifically, catalyzes the desaturation of fatty acids heptanoyl-CoA (C7), nonanoyl-CoA (C9), dodecanoyl-CoA (C12) and to a lesser extent pentanoyl-CoA (C5) and hexadecanoyl-CoA (C16), and hydroxylated fatty acid hydroxynonanoyl-CoA (PubMed:25775534, PubMed:29537254, PubMed:27551084). Also, catalyzes the desaturation fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior (PubMed:20610393, PubMed:25775534, PubMed:29537254, PubMed:29863473, PubMed:27551084). Specifically, shortens ascaroside with 5-carbon omega side chain (asc-omega-C5), 7-carbon side chain (asc-C7), 9-carbon side chain (asc-C9), 11-carbon side chain (asc-C11), 13-carbon side chain (asc-C13), 15-carbon side chain (asc-C15) and to a lesser extent ascarosides with 7-omega-carbon side chain (asc-omega-C7) (PubMed:25775534, PubMed:29537254, PubMed:27551084). Also shortens indol-3-carbonyl(IC)-ascarosides with 7-carbon side chain (IC-asc-C7) and to a lesser extent (IC)-ascarosides with 9-carbon side chain (IC-asc-C9) (PubMed:29863473). May associate and regulate the folding and/or the catalytic activity of other acyl-coenzyme A oxidases including acox-1.2, acox-1.3, acox-1.4 and acox-3 modulating the type of ascarosides produced (PubMed:25775534, PubMed:29537254, PubMed:29863473). In association with acox-1.3, catalyzes the desaturation of asc-C7-CoA but not of fatty acids or hydroxylated fatty acids (PubMed:25775534). Involved in the biosynthesis of asc-C6-MK (daumone 2) and asc-delta-C9 (daumone 3) but not asc-C7 (daumone 1); daumones are pheromones produced during unfavourable growth conditions which promote entry into the dauer stage (PubMed:20610393).<ref>PMID:20610393</ref> <ref>PMID:25775534</ref> <ref>PMID:27551084</ref> <ref>PMID:29537254</ref> <ref>PMID:29863473</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: Caeel]]
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bruner, S D]]
[[Category: Bruner SD]]
[[Category: Butcher, R A]]
[[Category: Butcher RA]]
[[Category: Jones, R A]]
[[Category: Jones RA]]
[[Category: Li, K]]
[[Category: Li K]]
[[Category: Zhang, X]]
[[Category: Zhang X]]
[[Category: Ascaroside]]
[[Category: Atp]]
[[Category: B-oxidation]]
[[Category: Dauer pheromone]]
[[Category: Oxidoreductase]]
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