PMID:10673437

Citation	Davies, C, Heath, RJ, White, SW and Rock, CO (2000) The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli. Structure 8:185-95
Abstract	beta-Ketoacyl-acyl carrier protein synthase III (FabH) initiates elongation in type II fatty acid synthase systems found in bacteria and plants. FabH is a ubiquitous component of the type II system and is positioned ideally in the pathway to control the production of fatty acids. The elucidation of the structure of FabH is important for the understanding of its regulation by feedback inhibition and its interaction with drugs. Although the structures of two related condensing enzymes are known, the roles of the active-site residues have not been experimentally tested.
Links	PubMed
Keywords	3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/chemistry; 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/genetics; 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/metabolism; Amino Acid Sequence; Base Sequence; Binding Sites; Catalysis; Crystallography, X-Ray; DNA Primers; Escherichia coli/enzymology; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation
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