6H9A

Crystal structure of anaerobic ergothioneine biosynthesis enzyme from Chlorobium limicola in complex with natural substrate trimethyl histidine.

6H9A の概要

• エントリーDOI: 10.2210/pdb6h9a/pdb
• 分子名称: Sulfurtransferase, N,N,N-trimethyl-histidine, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: metabolic role: anaerobic ergothioneine biosynthesis chemical activity: sulfur transfer, c-s bond formation protein family: rhodanese-like enzyme (pf00581), transferase
• 由来する生物種: Chlorobium limicola
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50450.20

構造登録者

Leisinger, F.,Burn, R.,Meury, M.,Lukat, P.,Seebeck, F.P. (登録日: 2018-08-03, 公開日: 2019-06-12, 最終更新日: 2024-05-15)

主引用文献

Leisinger, F.,Burn, R.,Meury, M.,Lukat, P.,Seebeck, F.P.
Structural and Mechanistic Basis for Anaerobic Ergothioneine Biosynthesis.
J.Am.Chem.Soc., 141:6906-6914, 2019

PubMed Abstract: Ergothioneine is an emergent factor in cellular redox biochemistry in humans and pathogenic bacteria. Broad consensus has formed around the idea that ergothioneine protects cells against reactive oxygen species. The recent discovery that anaerobic microorganisms make the same metabolite using oxygen-independent chemistry indicates that ergothioneine also plays physiological roles under anoxic conditions. In this report, we describe the crystal structure of the anaerobic ergothioneine biosynthetic enzyme EanB from green sulfur bacterium Chlorobium limicola. This enzyme catalyzes the oxidative sulfurization of N-α-trimethyl histidine. On the basis of structural and kinetic evidence, we describe the catalytic mechanism of this unusual C-S bond-forming reaction. Significant active-site conservation among distant EanB homologues suggests that the oxidative sulfurization of heterocyclic substrates may occur in a broad range of bacteria.

PubMed: 30943021
DOI: 10.1021/jacs.8b12596

実験手法

X-RAY DIFFRACTION (2.831 Å)