8XKZ
Core region of the citrate-induced human acetyl-CoA carboxylase 1 filament (ACC1-citrate)
Summary for 8XKZ
| Entry DOI | 10.2210/pdb8xkz/pdb |
| EMDB information | 38432 |
| Descriptor | Acetyl-CoA carboxylase 1, BIOTIN (2 entities in total) |
| Functional Keywords | biotin-dependent carboxylase, ligase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 509375.25 |
| Authors | Zhou, F.Y.,Zhang, Y.Y.,Zhou, Q.,Hu, Q. (deposition date: 2023-12-25, release date: 2024-10-23, Last modification date: 2024-11-06) |
| 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 Cited by 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: 39383219DOI: 10.1126/sciadv.ado4880 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.55 Å) |
Structure validation
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