1B3N

BETA-KETOACYL CARRIER PROTEIN SYNTHASE AS A DRUG TARGET, IMPLICATIONS FROM THE CRYSTAL STRUCTURE OF A COMPLEX WITH THE INHIBITOR CERULENIN.

1B3N の概要

• エントリーDOI: 10.2210/pdb1b3n/pdb
• 分子名称: PROTEIN (KETOACYL ACYL CARRIER PROTEIN SYNTHASE 2), (2S, 3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE (3 entities in total)
• 機能のキーワード: condensing enzymes, fatty acid elongation, cerulenin inhibition, lipid metabolism, drug design, drug target
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43183.72

構造登録者

Moche, M.,Schneider, G.,Edwards, P.,Dehesh, K.,Lindqvist, Y. (登録日: 1998-12-14, 公開日: 1999-04-06, 最終更新日: 2024-10-16)

主引用文献

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

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: 10037680
DOI: 10.1074/jbc.274.10.6031

実験手法

X-RAY DIFFRACTION (2.65 Å)