ArticleNature communications2023
C-N bond formation by a polyketide synthase.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Rigid polyanion architectures enable multiple ion-transport pathways and nanocluster dynamics in composite polymer battery electrolytes.Nature nanotechnology · 2026Article
- Fatty acid addition strategy redirected the metabolic flux towards an ultra-high monensin productivity ofSynthetic and systems biotechnology · 2025Article
- Article
- Cryo-electron microscopy structure of the di-domain core ofMicrobiology (Reading, England) · 2024Article
- Architecture of full-length type I modular polyketide synthases revealed by X-ray crystallography, cryo-electron microscopy, and AlphaFold2.Natural product reports · 2024Review
- No job too small for a giant enzyme.Nature chemical biology · 2023Article
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Authors and funding
15 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly-line polyketide synthases (PKSs) are molecular factories that produce diverse metabolites with wide-ranging biological activities. PKSs usually work by constructing and modifying the polyketide backbone successively. Here, we present the cryo-EM structure of CalA3, a chain release PKS module without an ACP domain, and its structures with amidation or hydrolysis products. The domain organization reveals a unique "∞"-shaped dimeric architecture with five connected domains. The catalytic region tightly contacts the structural region, resulting in two stabilized chambers with nearly perfect symmetry while the N-terminal docking domain is flexible. The structures of the ketosynthase (KS) domain illustrate how the conserved key residues that canonically catalyze C-C bond formation can be tweaked to mediate C-N bond formation, revealing the engineering adaptability of assembly-line polyketide synthases for the production of novel pharmaceutical agents.
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