4X8D

Ergothioneine-biosynthetic sulfoxide synthase EgtB in complex with N,N-dimethyl-histidine and gamma-glutamyl-cysteine

4X8D の概要

• エントリーDOI: 10.2210/pdb4x8d/pdb
• 関連するPDBエントリー: 4X8B 4X8E
• 分子名称: Sulfoxide synthase EgtB, GAMMA-GLUTAMYLCYSTEINE, N,N-dimethyl-L-histidine, ... (9 entities in total)
• 機能のキーワード: sulfoxide synthase, ergothioneine biosynthesis, c-lectin, dinb, non-heme fe(ii) enzyme, oxidoreductase
• 由来する生物種: Mycobacterium thermoresistibile ATCC 19527
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 100869.80

構造登録者

Vit, A.,Goncharenko, K.V.,Blankenfeldt, W.,Seebeck, F.P. (登録日: 2014-12-10, 公開日: 2015-01-28, 最終更新日: 2024-11-13)

主引用文献

Goncharenko, K.V.,Vit, A.,Blankenfeldt, W.,Seebeck, F.P.
Structure of the Sulfoxide Synthase EgtB from the Ergothioneine Biosynthetic Pathway.
Angew.Chem.Int.Ed.Engl., 54:2821-2824, 2015

PubMed Abstract: The non-heme iron enzyme EgtB catalyzes O2 -dependent C-S bond formation between γ-glutamyl cysteine and N-α-trimethyl histidine as the central step in ergothioneine biosynthesis. Both, the catalytic activity and the architecture of EgtB are distinct from known sulfur transferases or thiol dioxygenases. The crystal structure of EgtB from Mycobacterium thermoresistibile in complex with γ-glutamyl cysteine and N-α-trimethyl histidine reveals that the two substrates and three histidine residues serve as ligands in an octahedral iron binding site. This active site geometry is consistent with a catalytic mechanism in which C-S bond formation is initiated by an iron(III)-complexed thiyl radical attacking the imidazole ring of N-α-trimethyl histidine.

PubMed: 25597398
DOI: 10.1002/anie.201410045

実験手法

X-RAY DIFFRACTION (1.98 Å)