1Q7C

The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment

1Q7C の概要

• エントリーDOI: 10.2210/pdb1q7c/pdb
• 関連するPDBエントリー: 1Q7B
• 分子名称: 3-oxoacyl-[acyl-carrier protein] reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: oxoacyl reductase; nadp+; crystal structure, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52633.40

構造登録者

Price, A.C.,Zhang, Y.-M.,Rock, C.O.,White, S.M. (登録日: 2003-08-17, 公開日: 2004-02-17, 最終更新日: 2024-02-21)

主引用文献

Price, A.C.,Zhang, Y.-M.,Rock, C.O.,White, S.M.
Cofactor-Induced Conformational Rearrangements Establish a Catalytically Competent Active Site and a Proton Relay Conduit in FabG
Structure, 12:417-428, 2004

PubMed Abstract: beta-Ketoacyl-acyl carrier protein reductase (FabG) is a key component in the type II fatty acid synthase system. The structures of Escherichia coli FabG and the FabG[Y151F] mutant in binary complexes with NADP(H) reveal that mechanistically important conformational changes accompany cofactor binding. The active site Ser-Tyr-Lys triad is repositioned into a catalytically competent constellation, and a hydrogen bonded network consisting of ribose hydroxyls, the Ser-Tyr-Lys triad, and four water molecules creates a proton wire to replenish the tyrosine proton donated during catalysis. Also, a disordered loop in FabG forms a substructure in the complex that shapes the entrance to the active site. A key observation is that the nicotinamide portion of the cofactor is disordered in the FabG[Y151F].NADP(H) complex, and Tyr151 appears to be necessary for high-affinity cofactor binding. Biochemical data confirm that FabG[Y151F] is defective in NADPH binding. Finally, structural changes consistent with the observed negative cooperativity of FabG are described.

PubMed: 15016358
DOI: 10.1016/j.str.2004.02.008

実験手法

X-RAY DIFFRACTION (2.5 Å)