Fayang Zhou

Oct 9, 2024 | science.org | Deborah Carper |Hyun Lee |Nolan Tucker |Fayang Zhou

AbstractHuman 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.

Jun 17, 2024 | biorxiv.org | Fayang Zhou |Yuanyuan Zhang |Yuyao Zhu |Qiang Zhou

AbstractHuman acetyl-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-EM structure of human ACC1 in its inactive state, which forms a unique filament structure and is in complex with acetyl-CoA.

May 2, 2024 | biorxiv.org | Yuanyuan Zhang |Yuyao Zhu |Qiang Zhou |Fayang Zhou

AbstractPropionyl-CoA carboxylase (PCC) and 3-methylcrotonyl-CoA carboxylase (MCC) are biotin-dependent carboxylases (BDCs) that catalyze the metabolism of odd-chain fatty acids, cholesterol, and specific amino acids. For human PCC and MCC, only a low-resolution (15 Å) three-dimensional structure of human PCC has been reported. Here, we report high-resolution (2.29–3.28 Å) cryo-EM structures of human PCC and MCC holoenzymes in their apo and acetyl-CoA and propionyl-CoA-bound states.