ArticleNature structural & molecular biology2025
Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Affinity purification contaminants identified by cryo-EM and mass spectrometry.Bioscience reports · 2026Article
- Architecture of an asymmetric short chain/long chain hybrid acyl‑CoA carboxylase from Mycobacterium smegmatis.Communications biology · 2026Article
- Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Substrate-enhanced filamentation of 3-methylcrotonyl-CoA carboxylase inbioRxiv : the preprint server for biology · 2025Article
- LncBADR promotes T cell-mediated autoimmunity by binding Mccc1 and Pcca to regulate BCAAs degradation.Journal of neuroinflammation · 2025Article
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Authors and funding
8 authors.
Funding
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Abstract
The enzymes 3-methylcrotonyl-coenzyme A (CoA) carboxylase (MCC), pyruvate carboxylase and propionyl-CoA carboxylase belong to the biotin-dependent carboxylase family located in mitochondria. They participate in various metabolic pathways in human such as amino acid metabolism and tricarboxylic acid cycle. Many human diseases are caused by mutations in those enzymes but their structures have not been fully resolved so far. Here we report an optimized purification strategy to obtain high-resolution structures of intact human endogenous MCC, propionyl-CoA carboxylase and pyruvate carboxylase in different conformational states. We also determine the structures of MCC bound to different substrates. Analysis of MCC structures in different states reveals the mechanism of the substrate-induced, multi-element synergistic activation of MCC. These results provide important insights into the catalytic mechanism of the biotin-dependent carboxylase family and are of great value for the development of new drugs for the treatment of related diseases.
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Registered trials
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