ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structure-based analysis of the molecular interactions between acyltransferase and acyl carrier protein in vicenistatin biosynthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 92 citations in OpenAlex.
- Ancestral sequence reconstruction as a tool for structural analysis of modular polyketide synthases.Nature communications · 2025Article
- Structure of a putative terminal amidation domain in natural product biosynthesis.Structure (London, England : 1993) · 2025Article
- Elucidation of interface interactions between a dehydratase domain and an acyl carrier protein in cremimycin polyketide synthase.FEBS letters · 2025Article
- The structure of full-length AFPK supports the ACP linker in a role that regulates iterative polyketide and fatty acid assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Structure-function analysis of carrier protein-dependent 2-sulfamoylacetyl transferase in the biosynthesis of altemicidin.Nature communications · 2024Article
- Architecture of full-length type I modular polyketide synthases revealed by X-ray crystallography, cryo-electron microscopy, and AlphaFold2.Natural product reports · 2024Review
- Biosynthesis of macrolactam antibiotics with β-amino acid polyketide starter units.The Journal of antibiotics · 2024Review
- Structure and Mechanisms of Assembly-Line Polyketide Synthases.Annual review of biochemistry · 2024Review
- Semi-synthesis and structure-activity relationship study yield antibacterial vicenistatin derivatives with low cytotoxicity.The Journal of antibiotics · 2024Article
- Conformational Changes of Acyl Carrier Protein Switch the Chain Length Preference of Acyl-ACP Thioesterase ChFatB2.International journal of molecular sciences · 2023Article
- Characterization of three succinyl-CoA acyltransferases involved in polyketide chain assembly.Applied microbiology and biotechnology · 2023Article
- Enzymology of assembly line synthesis by modular polyketide synthases.Nature chemical biology · 2023Review
- Protein-Protein Recognition Involved in the Intermodular Transacylation Reaction in Modular Polyketide Synthase in the Biosynthesis of Vicenistatin.Chembiochem : a European journal of chemical biology · 2022Article
- Polyene Macrolactams from Marine and Terrestrial Sources: Structure, Production Strategies, Biosynthesis and Bioactivities.Marine drugs · 2022Review
- Structure of putative tumor suppressor ALDH1L1.Communications biology · 2022Article
- Article
- Modular polyketide synthase contains two reaction chambers that operate asynchronously.Science (New York, N.Y.) · 2021Article
- Complex structure of the acyltransferase VinK and the carrier protein VinL with a pantetheine cross-linking probe.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Engineering the acyltransferase domain of epothilone polyketide synthase to alter the substrate specificity.Microbial cell factories · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acyltransferases (ATs) are key determinants of building block specificity in polyketide biosynthesis. Despite the importance of protein-protein interactions between AT and acyl carrier protein (ACP) during the acyltransfer reaction, the mechanism of ACP recognition by AT is not understood in detail. Herein, we report the crystal structure of AT VinK, which transfers a dipeptide group between two ACPs, VinL and VinP1LdACP, in vicenistatin biosynthesis. The isolated VinK structure showed a unique substrate-binding pocket for the dipeptide group linked to ACP. To gain greater insight into the mechanism of ACP recognition, we attempted to crystallize the VinK-ACP complexes. Because transient enzyme-ACP complexes are difficult to crystallize, we developed a covalent cross-linking strategy using a bifunctional maleimide reagent to trap the VinK-ACP complexes, allowing the determination of the crystal structure of the VinK-VinL complex. In the complex structure, Arg-153, Met-206, and Arg-299 of VinK interact with the negatively charged helix II region of VinL. The VinK-VinL complex structure allows, to our knowledge, the first visualization of the interaction between AT and ACP and provides detailed mechanistic insights into ACP recognition by AT.
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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.