5i6f: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
'''Unreleased structure'''


The entry 5i6f is ON HOLD  until Paper Publication
==Crystal structure of C-terminal variant 1 of Chaetomium thermophilum acetyl-CoA carboxylase==
<StructureSection load='5i6f' size='340' side='right' caption='[[5i6f]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5i6f]] is a 2 chain structure. 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>
</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]], [[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'>[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]</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.


Authors: Hunkeler, M., Stuttfeld, E., Hagmann, A., Imseng, I., Maier, T.
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Stuttfeld, E]]
<div class="pdbe-citations 5i6f" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hagmann, A]]
[[Category: Hunkeler, M]]
[[Category: Hunkeler, M]]
[[Category: Imseng, S]]
[[Category: Maier, T]]
[[Category: Maier, T]]
[[Category: Imseng, I]]
[[Category: Stuttfeld, E]]
[[Category: Hagmann, A]]
[[Category: Carboxylase]]
[[Category: Carrier protein-dependent enzyme]]
[[Category: Fatty acid metabolism]]
[[Category: Ligase]]
[[Category: Multienzyme]]
Retrieved from "https://proteopedia.org/5i6f"