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| | ==Crystal structure of C-terminal variant 1 of Chaetomium thermophilum acetyl-CoA carboxylase== | | ==Crystal structure of C-terminal variant 1 of Chaetomium thermophilum acetyl-CoA carboxylase== |
| - | <StructureSection load='5i6f' size='340' side='right' caption='[[5i6f]], [[Resolution|resolution]] 3.60Å' scene=''> | + | <StructureSection load='5i6f' size='340' side='right'caption='[[5i6f]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5i6f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I6F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i6f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I6F FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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]] 3.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5i6e|5i6e]], [[5i6g|5i6g]], [[5i6h|5i6h]], [[5i6i|5i6i]], [[5i87|5i87]]</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=5i6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i6f OCA], [https://pdbe.org/5i6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i6f RCSB], [https://www.ebi.ac.uk/pdbsum/5i6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i6f ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0021690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</td></tr>
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| - | <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=5i6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i6f OCA], [http://pdbe.org/5i6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i6f RCSB], [http://www.ebi.ac.uk/pdbsum/5i6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i6f ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0S3L5_CHATD G0S3L5_CHATD] |
| | <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: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| - | [[Category: Hagmann, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Hunkeler, M]] | + | [[Category: Hagmann A]] |
| - | [[Category: Imseng, S]] | + | [[Category: Hunkeler M]] |
| - | [[Category: Maier, T]] | + | [[Category: Imseng S]] |
| - | [[Category: Stuttfeld, E]] | + | [[Category: Maier T]] |
| - | [[Category: Carboxylase]]
| + | [[Category: Stuttfeld E]] |
| - | [[Category: Carrier protein-dependent enzyme]]
| + | |
| - | [[Category: Fatty acid metabolism]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Multienzyme]]
| + | |
| Structural highlights
Function
G0S3L5_CHATD
Publication Abstract from PubMed
Acetyl-CoA carboxylases (ACCs) catalyse the committed step in fatty-acid biosynthesis: the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. They are important regulatory hubs for metabolic control and relevant drug targets for the treatment of the metabolic syndrome and cancer. Eukaryotic ACCs are single-chain multienzymes characterized by a large, non-catalytic central domain (CD), whose role in ACC regulation remains poorly characterized. Here we report the crystal structure of the yeast ACC CD, revealing a unique four-domain organization. A regulatory loop, which is phosphorylated at the key functional phosphorylation site of fungal ACC, wedges into a crevice between two domains of CD. Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. In contrast to related carboxylases, large-scale conformational changes are required for substrate turnover, and are mediated by the CD under phosphorylation control.
The dynamic organization of fungal acetyl-CoA carboxylase.,Hunkeler M, Stuttfeld E, Hagmann A, Imseng S, Maier T Nat Commun. 2016 Apr 13;7:11196. doi: 10.1038/ncomms11196. PMID:27073141[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hunkeler M, Stuttfeld E, Hagmann A, Imseng S, Maier T. The dynamic organization of fungal acetyl-CoA carboxylase. Nat Commun. 2016 Apr 13;7:11196. doi: 10.1038/ncomms11196. PMID:27073141 doi:http://dx.doi.org/10.1038/ncomms11196
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