4y9j
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4y9j]] is a 2 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=4Y9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y9J FirstGlance]. <br> | <table><tr><td colspan='2'>[[4y9j]] is a 2 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=4Y9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y9J FirstGlance]. <br> | ||
| - | </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>, <scene name='pdbligand=UCC:S-{(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl}+undecanethioate'>UCC</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]] 1.8Å</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>, <scene name='pdbligand=UCC:S-{(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl}+undecanethioate'>UCC</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=4y9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y9j OCA], [https://pdbe.org/4y9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y9j RCSB], [https://www.ebi.ac.uk/pdbsum/4y9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y9j 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=4y9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y9j OCA], [https://pdbe.org/4y9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y9j RCSB], [https://www.ebi.ac.uk/pdbsum/4y9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y9j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ACD11_CAEEL ACD11_CAEEL] Promotes adaption to elevated temperatures by regulating expression of the lipid desaturase, fat-7. Binds selectively and with high affinity to fatty acids with chain lengths from C10 to C12 and prevents them from activating fat-7 expression mediated by the nuclear hormone receptor nhr-49, leading to low levels of membrane lipid desaturation and membrane fluidity for adaption to heat.<ref>PMID:25981666</ref> | [https://www.uniprot.org/uniprot/ACD11_CAEEL ACD11_CAEEL] Promotes adaption to elevated temperatures by regulating expression of the lipid desaturase, fat-7. Binds selectively and with high affinity to fatty acids with chain lengths from C10 to C12 and prevents them from activating fat-7 expression mediated by the nuclear hormone receptor nhr-49, leading to low levels of membrane lipid desaturation and membrane fluidity for adaption to heat.<ref>PMID:25981666</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cells adapt to temperature shifts by adjusting levels of lipid desaturation and membrane fluidity. This fundamental process occurs in nearly all forms of life, but its mechanism in eukaryotes is unknown. We discovered that the evolutionarily conserved Caenorhabditis elegans gene acdh-11 (acyl-CoA dehydrogenase [ACDH]) facilitates heat adaptation by regulating the lipid desaturase FAT-7. Human ACDH deficiency causes the most common inherited disorders of fatty acid oxidation, with syndromes that are exacerbated by hyperthermia. Heat upregulates acdh-11 expression to decrease fat-7 expression. We solved the high-resolution crystal structure of ACDH-11 and established the molecular basis of its selective and high-affinity binding to C11/C12-chain fatty acids. ACDH-11 sequesters C11/C12-chain fatty acids and prevents these fatty acids from activating nuclear hormone receptors and driving fat-7 expression. Thus, the ACDH-11 pathway drives heat adaptation by linking temperature shifts to regulation of lipid desaturase levels and membrane fluidity via an unprecedented mode of fatty acid signaling. | ||
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| - | Acyl-CoA Dehydrogenase Drives Heat Adaptation by Sequestering Fatty Acids.,Ma DK, Li Z, Lu AY, Sun F, Chen S, Rothe M, Menzel R, Sun F, Horvitz HR Cell. 2015 May 21;161(5):1152-63. doi: 10.1016/j.cell.2015.04.026. Epub 2015 May , 14. PMID:25981666<ref>PMID:25981666</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4y9j" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Crystal Structure of Caenorhabditis elegans ACDH-11 in complex with C11-CoA
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