ArticleNature chemistry2020
Structural snapshots of the minimal PKS system responsible for octaketide biosynthesis.
Article in Nature chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 56 citations in OpenAlex.
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- Crystal structure of the type VI secretion system adaptor protein Tla3 from Pseudomonas aeruginosa.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Unveiling Putative Functions of Burkholderia pseudomallei K96243 Hypothetical Proteins Via High-Throughput Characterization of Structural Similarities.Interdisciplinary sciences, computational life sciences · 2026Article
- Structural Diversity and Bioactivities of Mangrove-Derived Fungal Polyketids (2020-2025).Marine drugs · 2025Review
- Development of a High Anthraquinone-ProducingACS synthetic biology · 2025Article
- A Phosphopantetheinyl Transferase fromACS omega · 2025Article
- The Isopropylstilbene Precursor Cinnamic Acid Inhibits Anthraquinone Pigment Production by Targeting AntI.Journal of the American Chemical Society · 2025Article
- Elucidating the Iterative Elongation Mechanism in a Type III Polyketide Synthase.Journal of the American Chemical Society · 2025Article
- MultiT2: A Tool Connecting the Multimodal Data for Bacterial Aromatic Polyketide Natural Products.ACS omega · 2025Article
- Strategic Acyl Carrier Protein Engineering Enables Functional Type II Polyketide Synthase Reconstitution In Vitro.ACS chemical biology · 2025Article
- Exploring the compatibility of phosphopantetheinyl transferases with acyl carrier proteins spanning type II polyketide synthase sequence space.Journal of industrial microbiology & biotechnology · 2024Article
- Analysis of the Setomimycin Biosynthetic Gene Cluster fromInternational journal of molecular sciences · 2024Article
- Polyketide Trimming Shapes Dihydroxynaphthalene-Melanin and Anthraquinone Pigments.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structural and mechanistic insights into Quinolone Synthase to address its functional promiscuity.Communications biology · 2024Article
- Simultaneous DHA and organic selenium production by Schizochytrium sp.: a theoretical basis.Scientific reports · 2023Article
- Metabolic Engineering and Synthetic Biology Approaches for the Heterologous Production of Aromatic Polyketides.International journal of molecular sciences · 2023Review
- Enzymology of assembly line synthesis by modular polyketide synthases.Nature chemical biology · 2023Review
- C-N bond formation by a polyketide synthase.Nature communications · 2023Article
- Priming enzymes from the pikromycin synthase reveal how assembly-line ketosynthases catalyze carbon-carbon chemistry.Structure (London, England : 1993) · 2022Article
- Unprecedented Mushroom Polyketide Synthases Produce the Universal Anthraquinone Precursor.Angewandte Chemie (International ed. in English) · 2022Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type II polyketide synthases (PKSs) are multi-enzyme complexes that produce secondary metabolites of medical relevance. Chemical backbones of such polyketides are produced by minimal PKS systems that consist of a malonyl transacylase, an acyl carrier protein and an α/β heterodimeric ketosynthase. Here, we present X-ray structures of all ternary complexes that constitute the minimal PKS system for anthraquinone biosynthesis in Photorhabdus luminescens. In addition, we characterize this invariable core using molecular simulations, mutagenesis experiments and functional assays. We show that malonylation of the acyl carrier protein is accompanied by major structural rearrangements in the transacylase. Principles of an ongoing chain elongation are derived from the ternary complex with a hexaketide covalently linking the heterodimeric ketosynthase with the acyl carrier protein. Our results for the minimal PKS system provide mechanistic understanding of PKSs and a fundamental basis for engineering PKS pathways for future applications.
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