1KAS

BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI

1KAS の概要

• エントリーDOI: 10.2210/pdb1kas/pdb
• 分子名称: BETA-KETOACYL ACP SYNTHASE II (2 entities in total)
• 機能のキーワード: acyltransferase, condensing enzyme, fatty acid elongation, lipid metabolism, alpha-beta protein, five-layered fold, alpha-beta-alpha-beta-alpha
• 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: 42958.43

構造登録者

Huang, W.,Jia, J.,Edwards, P.,Dehesh, K.,Schneider, G.,Lindqvist, Y. (登録日: 1997-12-22, 公開日: 1999-03-02, 最終更新日: 2024-02-07)

主引用文献

Huang, W.,Jia, J.,Edwards, P.,Dehesh, K.,Schneider, G.,Lindqvist, Y.
Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.
EMBO J., 17:1183-1191, 1998

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 crystal structure of beta-ketoacyl synthase II from Escherichia coli has been determined with the multiple isomorphous replacement method and refined at 2.4 A resolution. The subunit consists of two mixed five-stranded beta-sheets surrounded by alpha-helices. The two sheets are packed against each other in such a way that the fold can be described as consisting of five layers, alpha-beta-alpha-beta-alpha. The enzyme is a homodimer, and the subunits are related by a crystallographic 2-fold axis. The two active sites are located near the dimer interface but are approximately 25 A apart. The proposed nucleophile in the reaction, Cys163, is located at the bottom of a mainly hydrophobic pocket which is also lined with several conserved polar residues. In spite of very low overall sequence homology, the structure of beta-ketoacyl synthase is similar to that of thiolase, an enzyme involved in the beta-oxidation pathway, indicating that both enzymes might have a common ancestor.

PubMed: 9482715
DOI: 10.1093/emboj/17.5.1183

実験手法

X-RAY DIFFRACTION (2.4 Å)