|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4y9l' size='340' side='right'caption='[[4y9l]], [[Resolution|resolution]] 2.27Å' scene=''> | | <StructureSection load='4y9l' size='340' side='right'caption='[[4y9l]], [[Resolution|resolution]] 2.27Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y9l]] is a 2 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=4Y9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y9L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y9l]] 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=4Y9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y9L 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y9j|4y9j]]</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=4y9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y9l OCA], [https://pdbe.org/4y9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y9l RCSB], [https://www.ebi.ac.uk/pdbsum/4y9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y9l ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acdh-11, CELE_Y45F3A.3, Y45F3A.3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Very-long-chain_acyl-CoA_dehydrogenase Very-long-chain acyl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.9 1.3.8.9] </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=4y9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y9l OCA], [http://pdbe.org/4y9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y9l RCSB], [http://www.ebi.ac.uk/pdbsum/4y9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y9l ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == 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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Very-long-chain acyl-CoA dehydrogenase]]
| + | [[Category: Li ZJ]] |
| - | [[Category: Li, Z J]] | + | [[Category: Sun F]] |
| - | [[Category: Sun, F]] | + | [[Category: Zhai YJ]] |
| - | [[Category: Zhai, Y J]] | + | [[Category: Zhang K]] |
| - | [[Category: Zhang, K]] | + | |
| - | [[Category: Acyl-coa dehydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
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.[1]
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ma DK, Li Z, Lu AY, Sun F, Chen S, Rothe M, Menzel R, Sun F, Horvitz HR. Acyl-CoA Dehydrogenase Drives Heat Adaptation by Sequestering Fatty Acids. Cell. 2015 May 21;161(5):1152-63. doi: 10.1016/j.cell.2015.04.026. Epub 2015 May , 14. PMID:25981666 doi:http://dx.doi.org/10.1016/j.cell.2015.04.026
- ↑ Ma DK, Li Z, Lu AY, Sun F, Chen S, Rothe M, Menzel R, Sun F, Horvitz HR. Acyl-CoA Dehydrogenase Drives Heat Adaptation by Sequestering Fatty Acids. Cell. 2015 May 21;161(5):1152-63. doi: 10.1016/j.cell.2015.04.026. Epub 2015 May , 14. PMID:25981666 doi:http://dx.doi.org/10.1016/j.cell.2015.04.026
|
