ArticleNature chemical biology2025
Structural basis for intermodular communication in assembly-line polyketide biosynthesis.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Condensation-independent intramodular translocation mechanism of the trans-AT polyketide synthase assembly line.Nature chemical biology · 2026Article
- Repurposing FDA-Approved Drugs to Inhibit Fungal PPTases for Broad-Spectrum Synergy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- C-terminal dimerization motifs control asynchronous chain elongation during modular polyketide biosynthesis.The Journal of biological chemistry · 2026Article
- Investigation of Domain-Domain Interaction between Acyl Carrier Protein and Thioesterase in Modular Polyketide Synthases.JACS Au · 2026Article
- Serendipity and the Slime Mold: A Visual Survey of High-Molecular-Weight Protein Assemblies Reveals the Structure of the Polyketide Synthase Pks16.Molecular & cellular proteomics : MCP · 2026Article
- Engineering of FK520 polyketide synthase for rapid access to quality control reference standards.Microbial cell factories · 2025Article
- Protein-Protein Complex Stability Controls Substrate Scope in a β-Ketoacyl-ACP Reductase Specific for Medium Chains.Angewandte Chemie (International ed. in English) · 2025Article
- Visualizing acyl carrier protein interactions within a crosslinked type I polyketide synthase.Nature communications · 2025Article
- Ancestral sequence reconstruction as a tool for structural analysis of modular polyketide synthases.Nature communications · 2025Article
- Distinct Acyl Carrier Protein Docking Sites Help Mediate the Opposite Stereoselectivities of A- and B-type Modular Polyketide Synthase Ketoreductases.Biochemistry · 2025Article
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Authors and funding
6 authors.
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Abstract
Assembly-line polyketide synthases (PKSs) are modular multi-enzyme systems with considerable potential for genetic reprogramming. Understanding how they selectively transport biosynthetic intermediates along a defined sequence of active sites could be harnessed to rationally alter PKS product structures. To investigate functional interactions between PKS catalytic and substrate acyl carrier protein (ACP) domains, we employed a bifunctional reagent to crosslink transient domain-domain interfaces of a prototypical assembly line, the 6-deoxyerythronolide B synthase, and resolved their structures by single-particle cryogenic electron microscopy (cryo-EM). Together with statistical per-particle image analysis of cryo-EM data, we uncovered interactions between ketosynthase (KS) and ACP domains that discriminate between intra-modular and inter-modular communication while reinforcing the relevance of conformational asymmetry during the catalytic cycle. Our findings provide a foundation for the structure-based design of hybrid PKSs comprising biosynthetic modules from different naturally occurring assembly lines.
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