ArticlePloS one2014
A polyketide synthase acyltransferase domain structure suggests a recognition mechanism for its hydroxymalonyl-acyl carrier protein substrate.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Prokaryotic PfaB is a terminal acyltransferase that determines the final PUFA product.Protein science : a publication of the Protein Society · 2026Article
- Evolutionary Reprogramming of Acyltransferase Domains in Polyene Macrolide Pathways.Microorganisms · 2026Article
- Module-Based Polyketide Synthase Engineering forACS synthetic biology · 2023Review
- A single amino acid residue controls acyltransferase activity in a polyketide synthase fromiScience · 2022Article
- Interfacial plasticity facilitates high reaction rate ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Active site labeling of fatty acid and polyketide acyl-carrier protein transacylases.Organic & biomolecular chemistry · 2019Article
- Extender Unit Promiscuity and Orthogonal Protein Interactions of an Aminomalonyl-ACP Utilizing Trans-Acyltransferase from Zwittermicin Biosynthesis.ACS chemical biology · 2018Article
- Acyltransferases as Tools for Polyketide Synthase Engineering.Antibiotics (Basel, Switzerland) · 2018Review
- Biosynthetic origin of butyrolactol A, an antifungal polyketide produced by a marine-derivedBeilstein journal of organic chemistry · 2017Article
- Polyketide stereocontrol: a study in chemical biology.Beilstein journal of organic chemistry · 2017Review
- Structure-based analysis of the molecular interactions between acyltransferase and acyl carrier protein in vicenistatin biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Recent advances in the biosynthesis of unusual polyketide synthase substrates.Natural product reports · 2016Review
- Recent Advances in Understanding and Engineering Polyketide Synthesis.F1000Research · 2016Review
- Biochemical and Structural Basis for Controlling Chemical Modularity in Fungal Polyketide Biosynthesis.Journal of the American Chemical Society · 2015Article
- Architecture of the polyketide synthase module: surprises from electron cryo-microscopy.Current opinion in structural biology · 2015Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
We have previously shown that the acyl transferase domain of ZmaA (ZmaA-AT) is involved in the biosynthesis of the aminopolyol polyketide/nonribosomal peptide hybrid molecule zwittermicin A from cereus UW85, and that it specifically recognizes the precursor hydroxymalonyl-acyl carrier protein (ACP) and transfers the hydroxymalonyl extender unit to a downstream second ACP via a transacylated AT domain intermediate. We now present the X-ray crystal structure of ZmaA-AT at a resolution of 1.7 Å. The structure shows a patch of solvent-exposed hydrophobic residues in the area where the AT is proposed to interact with the precursor ACP. We addressed the significance of the AT/ACP interaction in precursor specificity of the AT by testing whether malonyl- or methylmalonyl-ACP can be recognized by ZmaA-AT. We found that the ACP itself biases extender unit selection. Until now, structural information for ATs has been limited to ATs specific for the CoA-linked precursors malonyl-CoA and (2S)-methylmalonyl-CoA. This work contributes to polyketide synthase engineering efforts by expanding our knowledge of AT/substrate interactions with the structure of an AT domain that recognizes an ACP-linked substrate, the rare hydroxymalonate. Our structure suggests a model in which ACP interaction with a hydrophobic motif promotes secondary structure formation at the binding site, and opening of the adjacent substrate pocket lid to allow extender unit binding in the AT active site.
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