The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
Davies, C., Heath, R.J., White, S.W., Rock, C.O.(2000) Structure 8: 185-195
- PubMed: 10673437 
- DOI: https://doi.org/10.1016/s0969-2126(00)00094-0
- Primary Citation of Related Structures:  
1EBL - PubMed 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.
Organizational Affiliation: 
Department of Structural Biology, University of Tennessee, School of Biological Sciences, University of Sussex, Memphis, Falmer, 38163, BN1 9QG, USA, UK.