8XL1

Core region of the human acetyl-CoA carboxylase 1 filament in complex with acetyl-CoA (ACC1-inact)

Summary for 8XL1

• Entry DOI: 10.2210/pdb8xl1/pdb
• EMDB information: 38434
• Descriptor: Acetyl-CoA carboxylase 1, ACETYL COENZYME *A (2 entities in total)
• Functional Keywords: biotin-dependent carboxylase, ligase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 533357.89

Authors

Zhou, F.Y.,Zhang, Y.Y.,Zhou, Q.,Hu, Q. (deposition date: 2023-12-25, release date: 2024-10-23)

Primary citation

Zhou, F.,Zhang, Y.,Zhu, Y.,Zhou, Q.,Shi, Y.,Hu, Q.
Filament structures unveil the dynamic organization of human acetyl-CoA carboxylase.
Sci Adv, 10:eado4880-eado4880, 2024

PubMed Abstract: 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 Å. 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.

PubMed: 39383219
DOI: 10.1126/sciadv.ado4880

Experimental method

ELECTRON MICROSCOPY (2.57 Å)