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- Title
Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme
- Authors
Gajiwala, Ketan S.; Margosiak, Stephen; Lu, Jia; Cortez, Joseph; Su, Ying; Nie, Zhe; Appelt, Krzysztof
- Abstract
FabH (β-ketoacyl-acyl carrier protein synthase III) is unique in that it initiates fatty acid biosynthesis, is inhibited by long-chain fatty acids providing means for feedback control of the process, and dictates the fatty acid profile of the organism by virtue of its substrate specificity. We report the crystal structures of bacterial FabH enzymes from four different pathogenic species: Enterococcus faecalis, Haemophilus influenzae, Staphylococcus aureus and Escherichia coli. Structural data on the enzyme from different species show important differences in the architecture of the substrate-binding sites that parallel the inter-species diversity in the substrate specificities of these enzymes.
- Subjects
PROTEIN structure; CRYSTALS; CARRIER proteins; FATTY acids; BIOSYNTHESIS; FEEDBACK control systems; ENZYMES; ENTEROCOCCUS faecalis
- Publication
FEBS Letters, 2009, Vol 583, Issue 17, p2939
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.08.001