ArticleNature chemical biology2018
The structural organization of substrate loading in iterative polyketide synthases.
Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 65 citations in OpenAlex.
- Unraveling the FGFR-RNA splicing axis: Mechanisms, oncogenic crosstalks and innovations for therapeutic purpose.Acta pharmaceutica Sinica. B · 2026Review
- Bioactive Polyketides fromMarine drugs · 2025Review
- Structural basis for intermodular communication in assembly-line polyketide biosynthesis.Nature chemical biology · 2025Article
- Architecture of full-length type I modular polyketide synthases revealed by X-ray crystallography, cryo-electron microscopy, and AlphaFold2.Natural product reports · 2024Review
- Enzymology of assembly line synthesis by modular polyketide synthases.Nature chemical biology · 2023Review
- Structure and dynamics of the essential endogenous mycobacterial polyketide synthase Pks13.Nature structural & molecular biology · 2023Article
- Insights into azalomycin F assembly-line contribute to evolution-guided polyketide synthase engineering and identification of intermodular recognition.Nature communications · 2023Article
- The Ketosynthase Domain Controls Chain Length in Mushroom Oligocyclic Polyketide Synthases.Chembiochem : a European journal of chemical biology · 2023Article
- Mechanism-based cross-linking probes capture the Escherichia coli ketosynthase FabB in conformationally distinct catalytic states.Acta crystallographica. Section D, Structural biology · 2022Article
- Priming enzymes from the pikromycin synthase reveal how assembly-line ketosynthases catalyze carbon-carbon chemistry.Structure (London, England : 1993) · 2022Article
- Solution structure of the type I polyketide synthase Pks13 from Mycobacterium tuberculosis.BMC biology · 2022Article
- Article
- Underexplored bacteria as reservoirs of novel antimicrobial lipopeptides.Frontiers in chemistry · 2022Review
- Visualizing transiently associated catalytic domains in assembly-line biosynthesis using cryo-electron microscopy.Journal of structural biology · 2021Article
- Modular polyketide synthase contains two reaction chambers that operate asynchronously.Science (New York, N.Y.) · 2021Article
- Molecular basis for acyl carrier protein-ketoreductase interaction inChemical science · 2021Article
- Intrinsic and Extrinsic Programming of Product Chain Length and Release Mode in Fungal Collaborating Iterative Polyketide Synthases.Journal of the American Chemical Society · 2020Article
- Design, Synthesis, and Biophysical Evaluation of Mechanism-Based Probes for Condensation Domains of Nonribosomal Peptide Synthetases.ACS chemical biology · 2020Article
- Molecular basis of methylation and chain-length programming in a fungal iterative highly reducing polyketide synthase.Chemical science · 2019Article
- Modifying the Thioester Linkage Affects the Structure of the Acyl Carrier Protein.Angewandte Chemie (International ed. in English) · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Polyketide synthases (PKSs) are microbial multienzymes for the biosynthesis of biologically potent secondary metabolites. Polyketide production is initiated by the loading of a starter unit onto an integral acyl carrier protein (ACP) and its subsequent transfer to the ketosynthase (KS). Initial substrate loading is achieved either by multidomain loading modules or by the integration of designated loading domains, such as starter unit acyltransferases (SAT), whose structural integration into PKS remains unresolved. A crystal structure of the loading/condensing region of the nonreducing PKS CTB1 demonstrates the ordered insertion of a pseudodimeric SAT into the condensing region, which is aided by the SAT-KS linker. Cryo-electron microscopy of the post-loading state trapped by mechanism-based crosslinking of ACP to KS reveals asymmetry across the CTB1 loading/-condensing region, in accord with preferential 1:2 binding stoichiometry. These results are critical for re-engineering the loading step in polyketide biosynthesis and support functional relevance of asymmetric conformations of PKSs.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.