ArticleScientific reports2021
Structural comparison of Acinetobacter baumannii β-ketoacyl-acyl carrier protein reductases in fatty acid and aryl polyene biosynthesis.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Structural and dynamic roles of tandem acyl carrier proteins in aryl polyene biosynthesis in carbapenem-resistant Acinetobacter baumannii.Protein science : a publication of the Protein Society · 2025Article
- Exploring the microbial communities in coastal cenote and their hidden biotechnological potential.Microbial genomics · 2025Article
- Genomic insights into drug resistance and virulence determinants in rare pyomelanin-producing clinical isolates of Acinetobacter baumannii.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Article
- Genomic Insight intoPathogens (Basel, Switzerland) · 2025Article
- A comprehensive comparative genomic analysis revealed that plant growth promoting traits are ubiquitous in strains ofFrontiers in microbiology · 2024Article
- A comprehensive genomic analysis provides insights on the high environmental adaptability ofFrontiers in microbiology · 2023Article
- Enzymology of standalone elongating ketosynthases.Chemical science · 2022Review
- Of its five acyl carrier proteins, only AcpP1 functions inFrontiers in microbiology · 2022Article
- Structural basis of the complementary activity of two ketosynthases in aryl polyene biosynthesis.Scientific reports · 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
Some Gram-negative bacteria harbor lipids with aryl polyene (APE) moieties. Biosynthesis gene clusters (BGCs) for APE biosynthesis exhibit striking similarities with fatty acid synthase (FAS) genes. Despite their broad distribution among pathogenic and symbiotic bacteria, the detailed roles of the metabolic products of APE gene clusters are unclear. Here, we determined the crystal structures of the β-ketoacyl-acyl carrier protein (ACP) reductase ApeQ produced by an APE gene cluster from clinically isolated virulent Acinetobacter baumannii in two states (bound and unbound to NADPH). An in vitro visible absorption spectrum assay of the APE polyene moiety revealed that the β-ketoacyl-ACP reductase FabG from the A. baumannii FAS gene cluster cannot be substituted for ApeQ in APE biosynthesis. Comparison with the FabG structure exhibited distinct surface electrostatic potential profiles for ApeQ, suggesting a positively charged arginine patch as the cognate ACP-binding site. Binding modeling for the aryl group predicted that Leu185 (Phe183 in FabG) in ApeQ is responsible for 4-benzoyl moiety recognition. Isothermal titration and arginine patch mutagenesis experiments corroborated these results. These structure-function insights of a unique reductase in the APE BGC in comparison with FAS provide new directions for elucidating host-pathogen interaction mechanisms and novel antibiotics discovery.
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