View source for 8xl2


==Human acetyl-CoA carboxylase 1 filament in complex with acetyl-CoA (ACC1-inact)==
<StructureSection load='8xl2' size='340' side='right'caption='[[8xl2]], [[Resolution|resolution]] 2.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xl2]] is a 4 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=8XL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XL2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.73&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</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=8xl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xl2 OCA], [https://pdbe.org/8xl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xl2 RCSB], [https://www.ebi.ac.uk/pdbsum/8xl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xl2 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ACACA_HUMAN ACACA_HUMAN] Defects in ACACA are a cause of acetyl-CoA carboxylase 1 deficiency (ACACAD) [MIM:[https://omim.org/entry/613933 613933]; also known as ACAC deficiency or ACC deficiency. An inborn error of de novo fatty acid synthesis associated with severe brain damage, persistent myopathy and poor growth.<ref>PMID:6114432</ref> 
== Function ==
[https://www.uniprot.org/uniprot/ACACA_HUMAN ACACA_HUMAN] Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.<ref>PMID:20952656</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human acetyl-coenzyme A (CoA) carboxylases (ACCs) catalyze the carboxylation of acetyl-CoA, which is the rate-limiting step in fatty acid synthesis. The molecular mechanism underlying the dynamic organization of ACCs is largely unknown. Here, we determined the cryo-electron microscopy (EM) structure of human ACC1 in its inactive state, which forms a unique filament structure and is in complex with acetyl-CoA. We also determined the cryo-EM structure of human ACC1 activated by dephosphorylation and citrate treatment, at a resolution of 2.55 A. Notably, the covalently linked biotin binds to a site that is distant from the acetyl-CoA binding site when acetyl-CoA is absent, suggesting a potential coordination between biotin binding and acetyl-CoA binding. These findings provide insights into the structural dynamics and regulatory mechanisms of human ACCs.

Filament structures unveil the dynamic organization of human acetyl-CoA carboxylase.,Zhou F, Zhang Y, Zhu Y, Zhou Q, Shi Y, Hu Q Sci Adv. 2024 Oct 11;10(41):eado4880. doi: 10.1126/sciadv.ado4880. Epub 2024 Oct , 9. PMID:39383219<ref>PMID:39383219</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8xl2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Hu Q]]
[[Category: Zhang YY]]
[[Category: Zhou FY]]
[[Category: Zhou Q]]