1B3N
BETA-KETOACYL CARRIER PROTEIN SYNTHASE AS A DRUG TARGET, IMPLICATIONS FROM THE CRYSTAL STRUCTURE OF A COMPLEX WITH THE INHIBITOR CERULENIN.
Summary for 1B3N
| Entry DOI | 10.2210/pdb1b3n/pdb |
| Descriptor | PROTEIN (KETOACYL ACYL CARRIER PROTEIN SYNTHASE 2), (2S, 3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE (3 entities in total) |
| Functional Keywords | condensing enzymes, fatty acid elongation, cerulenin inhibition, lipid metabolism, drug design, drug target |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 43183.72 |
| Authors | Moche, M.,Schneider, G.,Edwards, P.,Dehesh, K.,Lindqvist, Y. (deposition date: 1998-12-14, release date: 1999-04-06, Last modification date: 2024-10-16) |
| Primary citation | Moche, M.,Schneider, G.,Edwards, P.,Dehesh, K.,Lindqvist, Y. Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase. J.Biol.Chem., 274:6031-6034, 1999 Cited by PubMed Abstract: 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. PubMed: 10037680DOI: 10.1074/jbc.274.10.6031 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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