The X-ray crystal structure of β-ketoacyl [acyl carrier protein] synthase I

被引：107

作者：

Olsen, JG

Kadziola, A

von Wettstein-Knowles, P

Siggaard-Andersen, M

Lindquist, Y

Larsen, S

机构：

[1] Univ Copenhagen, Inst Mol Biol, Dept Genet, DK-1353 Copenhagen, Denmark

[2] Univ Copenhagen, Ctr Crystallog Studies, DK-2100 Copenhagen, Denmark

[3] Karolinska Inst, Dept Med Biochem & Biophys, Div Struct Biol, S-17177 Stockholm, Sweden

来源：

FEBS LETTERS | 1999年 / 460卷 / 01期

关键词：

condensing enzyme; protein structure; fatty acid synthesis; Escherichia coli;

D O I：

10.1016/S0014-5793(99)01303-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of the fatty acid elongating enzyme beta-ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been determined to 2.3 Angstrom resolution by molecular replacement using the recently solved crystal structure of KAS II as a search model. The crystal contains two independent dimers in the asymmetric unit. KAS I assumes the thiolase alpha beta alpha beta alpha fold. Electrostatic potential distribution reveals an acyl carrier protein docking site and a presumed substrate binding pocket was detected extending the active site. Both subunits contribute to each substrate binding site in the dimer. (C) 1999 Federation of European Biochemical Societies.

引用

页码：46 / 52

页数：7

共 42 条

[1] A mechanism of drug action revealed by structural studies of enoyl reductase [J].