5i6i: Difference between revisions
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==Crystal structure of a dBCCP-variant of Chaetomium thermophilum acetyl-CoA carboxylase== | |||
<StructureSection load='5i6i' size='340' side='right' caption='[[5i6i]], [[Resolution|resolution]] 8.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5i6i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I6I 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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5i6e|5i6e]], [[5i6f|5i6f]], [[5i6g|5i6g]], [[5i6h|5i6h]], [[5i87|5i87]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </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=5i6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i6i OCA], [http://pdbe.org/5i6i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i6i RCSB], [http://www.ebi.ac.uk/pdbsum/5i6i PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:27073141</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5i6i" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acetyl-CoA carboxylase]] | |||
[[Category: Hagmann, A]] | |||
[[Category: Hunkeler, M]] | [[Category: Hunkeler, M]] | ||
[[Category: Imseng, S]] | [[Category: Imseng, S]] | ||
[[Category: Maier, T]] | [[Category: Maier, T]] | ||
[[Category: | [[Category: Stuttfeld, E]] | ||
[[Category: Carboxylase]] | |||
[[Category: Carrier protein-dependent enzyme]] | |||
[[Category: Fatty acid metabolism]] | |||
[[Category: Ligase]] | |||
[[Category: Multienzyme]] | |||
