EMD-38432
Core region of the citrate-induced human acetyl-CoA carboxylase 1 filament (ACC1-citrate)
EMD-38432
Single-particle2.55 Å
Deposition: 25/12/2023Map released: 23/10/2024
Last modified: 06/11/2024
Sample Organism:
Homo sapiens
Sample: Core region of the citrate-induced human acetyl-CoA carboxylase 1 filament (ACC1-citrate)
Fitted models: 8xkz (Avg. Q-score: 0.435)
Deposition Authors: Zhou FY, Zhang YY, Zhou Q
,
Hu Q
Sample: Core region of the citrate-induced human acetyl-CoA carboxylase 1 filament (ACC1-citrate)
Fitted models: 8xkz (Avg. Q-score: 0.435)
Deposition Authors: Zhou FY, Zhang YY, Zhou Q
,
Hu Q
Filament structures unveil the dynamic organization of human acetyl-CoA carboxylase.
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.
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.