ArticleScientific reports2017
Structural characterisation of the fatty acid biosynthesis enzyme FabF from the pathogen Listeria monocytogenes.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Understanding the role of pyruvate dehydrogenase inInfection and immunity · 2026Article
- Adaptive Tolerance of Listeria monocytogenes to Chemical Oxidants: Comparative Analysis of Transcriptomic Studies.Comprehensive reviews in food science and food safety · 2025Review
- Activity-based protein profiling guided new target identification of quinazoline derivatives for expediting bactericide discovery: Activity-based protein profiling derived new target discovery of antibacterial quinazolines.Journal of advanced research · 2025Article
- Screening of promising molecules against potential drug targets in Yersinia pestis by integrative pan and subtractive genomics, docking and simulation approach.Archives of microbiology · 2024Article
- Metabonomics and Transcriptomic Analysis of Free Fatty Acid Synthesis in Seedless and Tenera Oil Palm.International journal of molecular sciences · 2024Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
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Abstract
Development of new antimicrobial agents is required against the causative agent for listeriosis, Listeria monocytogenes, as the number of drug resistant strains continues to increase. A promising target is the β-ketoacyl-acyl carrier protein synthase FabF, which participates in the catalysis of fatty acid synthesis and elongation, and is required for the production of phospholipid membranes, lipoproteins, and lipopolysaccharides. In this study, we report the 1.35 Å crystal structure of FabF from L. monocytogenes, providing an excellent platform for the rational design of novel inhibitors. By comparing the structure of L. monocytogenes FabF with other published bacterial FabF structures in complex with known inhibitors and substrates, we highlight conformational changes within the active site, which will need to be accounted for during drug design and virtual screening studies. This high-resolution structure of FabF represents an important step in the development of new classes of antimicrobial agents targeting FabF for the treatment of listeriosis.
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