7YWC

Enzyme of biosynthetic pathway

7YWC の概要

• エントリーDOI: 10.2210/pdb7ywc/pdb
• 分子名称: Chorismate dehydratase, (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: enzyme activity, biosynthetic pathway, biosynthetic protein
• 由来する生物種: Streptomyces coelicolor
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66036.92

構造登録者

Archna, A.,Breithaupt, C.,Stubbs, M.T. (登録日: 2022-02-12, 公開日: 2022-10-26, 最終更新日: 2024-06-19)

主引用文献

Prasad, A.,Breithaupt, C.,Nguyen, D.A.,Lilie, H.,Ziegler, J.,Stubbs, M.T.
Mechanism of chorismate dehydratase MqnA, the first enzyme of the futalosine pathway, proceeds via substrate-assisted catalysis.
J.Biol.Chem., 298:102601-102601, 2022

PubMed Abstract: MqnA, the only chorismate dehydratase known so far, catalyzes the initial step in the biosynthesis of menaquinone via the futalosine pathway. Details of the MqnA reaction mechanism remain unclear. Here, we present crystal structures of Streptomyces coelicolor MqnA and its active site mutants in complex with chorismate and the product 3-enolpyruvyl-benzoate, produced during heterologous expression in Escherichia coli. Together with activity studies, our data are in line with dehydration proceeding via substrate assisted catalysis, with the enol pyruvyl group of chorismate acting as catalytic base. Surprisingly, structures of the mutant Asn17Asp with copurified ligand suggest that the enzyme converts to a hydrolase by serendipitous positioning of the carboxyl group. All complex structures presented here exhibit a closed Venus flytrap fold, with the enzyme exploiting the characteristic ligand binding properties of the fold for specific substrate binding and catalysis. The conformational rearrangements that facilitate complete burial of substrate/product, with accompanying topological changes to the enzyme surface, could foster substrate channeling within the biosynthetic pathway.

PubMed: 36265588
DOI: 10.1016/j.jbc.2022.102601

実験手法

X-RAY DIFFRACTION (1.917 Å)