1b3n
BETA-KETOACYL CARRIER PROTEIN SYNTHASE AS A DRUG TARGET, IMPLICATIONS FROM THE CRYSTAL STRUCTURE OF A COMPLEX WITH THE INHIBITOR CERULENIN.
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OverviewOverview
In the biosynthesis of fatty acids, the beta-ketoacyl-acyl carrier protein, (ACP) synthases catalyze chain elongation by the addition of two-carbon, units derived from malonyl-ACP to an acyl group bound to either ACP or, CoA. The enzyme is a possible drug target for treatment of certain cancers, and for tuberculosis. The crystal structure of the complex of the enzyme, from Escherichia coli, and the fungal mycotoxin cerulenin reveals that the, inhibitor is bound in a hydrophobic pocket formed at the dimer interface., Cerulenin is covalently attached to the active site cysteine through its, C2 carbon atom. The fit of the inhibitor to the active site is not, optimal, and there is thus room for improvement through structure based, design.
About this StructureAbout this Structure
1B3N is a Single protein structure of sequence from Escherichia coli with CER as ligand. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
ReferenceReference
Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase., Moche M, Schneider G, Edwards P, Dehesh K, Lindqvist Y, J Biol Chem. 1999 Mar 5;274(10):6031-4. PMID:10037680
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