8QFL

Ergothioneine dioxygenase from Thermocatellispora tengchongensis in complex with iron

8QFL の概要

• エントリーDOI: 10.2210/pdb8qfl/pdb
• 分子名称: Cysteine dioxygenase, FE (III) ION, ACETATE ION, ... (6 entities in total)
• 機能のキーワード: thiol dioxygenase ergothioneine dioxygenase, oxidoreductase
• 由来する生物種: Thermocatellispora tengchongensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41856.36

構造登録者

Vasseur, C.M.,Seebeck, F.P. (登録日: 2023-09-04, 公開日: 2023-12-27, 最終更新日: 2024-02-21)

主引用文献

Nalivaiko, E.Y.,Vasseur, C.M.,Seebeck, F.P.
Enzyme-Catalyzed Oxidative Degradation of Ergothioneine.
Angew.Chem.Int.Ed.Engl., 63:e202318445-e202318445, 2024

PubMed Abstract: Ergothioneine is a sulfur-containing metabolite that is produced by bacteria and fungi, and is absorbed by plants and animals as a micronutrient. Ergothioneine reacts with harmful oxidants, including singlet oxygen and hydrogen peroxide, and may therefore protect cells against oxidative stress. Herein we describe two enzymes from actinobacteria that cooperate in the specific oxidative degradation of ergothioneine. The first enzyme is an iron-dependent thiol dioxygenase that produces ergothioneine sulfinic acid. A crystal structure of ergothioneine dioxygenase from Thermocatellispora tengchongensis reveals many similarities with cysteine dioxygenases, suggesting that the two enzymes share a common mechanism. The second enzyme is a metal-dependent ergothioneine sulfinic acid desulfinase that produces Nα-trimethylhistidine and SO . The discovery that certain actinobacteria contain the enzymatic machinery for O -dependent biosynthesis and O -dependent degradation of ergothioneine indicates that these organisms may actively manage their ergothioneine content.

PubMed: 38095354
DOI: 10.1002/anie.202318445

実験手法

X-RAY DIFFRACTION (1.75 Å)