1I01

CRYSTAL STRUCTURE OF BETA-KETOACYL [ACYL CARRIER PROTEIN] REDUCTASE FROM E. COLI.

1I01 の概要

• エントリーDOI: 10.2210/pdb1i01/pdb
• 分子名称: BETA-KETOACYL [ACP] REDUCTASE (2 entities in total)
• 機能のキーワード: rossmann fold, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 204698.22

構造登録者

Price, A.C.,Rock, C.O.,White, S.W. (登録日: 2001-01-27, 公開日: 2001-02-07, 最終更新日: 2024-02-07)

主引用文献

Price, A.C.,Zhang, Y.M.,Rock, C.O.,White, S.W.
Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis.
Biochemistry, 40:12772-12781, 2001

PubMed Abstract: The structure of beta-ketoacyl-[acyl carrier protein] reductase (FabG) from Escherichia coli was determined via the multiwavelength anomalous diffraction technique using a selenomethionine-labeled crystal containing 88 selenium sites in the asymmetric unit. The comparison of the E. coli FabG structure with the homologous Brassica napus FabG.NADP(+) binary complex reveals that cofactor binding causes a substantial conformational change in the protein. This conformational change puts all three active-site residues (Ser 138, Tyr 151, and Lys 155) into their active configurations and provides a structural mechanism for allosteric communication between the active sites in the homotetramer. FabG exhibits negative cooperative binding of NADPH, and this effect is enhanced by the presence of acyl carrier protein (ACP). NADPH binding also increases the affinity and decreases the maximum binding of ACP to FabG. Thus, unlike other members of the short-chain dehydrogenase/reductase superfamily, FabG undergoes a substantial conformational change upon cofactor binding that organizes the active-site triad and alters the affinity of the other substrate-binding sites in the tetrameric enzyme.

PubMed: 11669613
DOI: 10.1021/bi010737g

実験手法

X-RAY DIFFRACTION (2.6 Å)