1TUV

Crystal structure of YgiN in complex with menadione

1TUV の概要

• エントリーDOI: 10.2210/pdb1tuv/pdb
• 関連するPDBエントリー: 1R6Y
• 分子名称: Protein ygiN, MENADIONE (3 entities in total)
• 機能のキーワード: menadione oxidase, monooxygenase, co-crystal with natural product, ferredoxin fold, unknown function
• 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: 12947.90

構造登録者

Adams, M.A.,Jia, Z. (登録日: 2004-06-25, 公開日: 2005-01-11, 最終更新日: 2024-02-14)

主引用文献

Adams, M.A.,Jia, Z.
Structural and Biochemical Evidence for an Enzymatic Quinone Redox Cycle in Escherichia coli: IDENTIFICATION OF A NOVEL QUINOL MONOOXYGENASE
J.Biol.Chem., 280:8358-8363, 2005

PubMed Abstract: Naturally synthesized quinones perform a variety of important cellular functions. Escherichia coli produce both ubiquinone and menaquinone, which are involved in electron transport. However, semiquinone intermediates produced during the one-electron reduction of these compounds, as well as through auto-oxidation of the hydroxyquinone product, generate reactive oxygen species that stress the cell. Here, we present the crystal structure of YgiN, a protein of hitherto unknown function. The three-dimensional fold of YgiN is similar to that of ActVA-Orf6 monooxygenase, which acts on hydroxyquinone substrates. YgiN shares a promoter with "modulator of drug activity B," a protein with activity similar to that of mammalian DT-diaphorase capable of reducing mendione. YgiN was able to reoxidize menadiol, the product of the "modulator of drug activity B" (MdaB) enzymatic reaction. We therefore refer to YgiN as quinol monooxygenase. Modulator of drug activity B is reported to be involved in the protection of cells from reactive oxygen species formed during single electron oxidation and reduction reactions. The enzymatic activities, together with the structural characterization of YgiN, lend evidence to the possible existence of a novel quinone redox cycle in E. coli.

PubMed: 15613473
DOI: 10.1074/jbc.M412637200

実験手法

X-RAY DIFFRACTION (1.7 Å)