Structural characterisation of the fatty acid biosynthesis enzyme FabF from the pathogen Listeria monocytogenes.

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.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Soares da Costa TP,Nanson JD,Forwood JK

doi

10.1038/srep39277

subject

Has Abstract

pub_date

2017-01-03 00:00:00

pages

39277

issn

2045-2322

pii

srep39277

journal_volume

7

pub_type

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