5i87: Difference between revisions
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New page: '''Unreleased structure''' The entry 5i87 is ON HOLD Authors: Stuttfeld, E., Hunkeler, M., Hagmann, A., Imseng, S., Maier, T. Description: Category: Unreleased Structures [[Catego... |
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==Crystal structure of BT-CD domains of human acetyl-CoA carboxylase== | |||
<StructureSection load='5i87' size='340' side='right'caption='[[5i87]], [[Resolution|resolution]] 3.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5i87]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I87 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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=5i87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i87 OCA], [https://pdbe.org/5i87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i87 RCSB], [https://www.ebi.ac.uk/pdbsum/5i87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i87 ProSAT]</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 5i87" style="background-color:#fffaf0;"></div> | ||
[[Category: Hunkeler | |||
[[Category: Imseng | ==See Also== | ||
[[Category: Maier | *[[Acetyl-CoA carboxylase 3D structures|Acetyl-CoA carboxylase 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Hagmann A]] | |||
[[Category: Hunkeler M]] | |||
[[Category: Imseng S]] | |||
[[Category: Maier T]] | |||
[[Category: Stuttfeld E]] | |||
