6O6M

The Structure of EgtB (Cabther)

6O6M の概要

• エントリーDOI: 10.2210/pdb6o6m/pdb
• 分子名称: EgtB (Cabther), FE (III) ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: non-heme iron dependent enzyme, ergothioneine, metal binding protein
• 由来する生物種: Chloracidobacterium thermophilum (strain B)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 209593.69

構造登録者

Irani, S.,Zhang, Y. (登録日: 2019-03-07, 公開日: 2019-07-31, 最終更新日: 2024-03-13)

主引用文献

Naowarojna, N.,Irani, S.,Hu, W.,Cheng, R.,Zhang, L.,Li, X.,Chen, J.,Zhang, Y.J.,Liu, P.
Crystal Structure of the Ergothioneine Sulfoxide Synthase fromCandidatus Chloracidobacterium thermophilumand Structure-Guided Engineering To Modulate Its Substrate Selectivity.
Acs Catalysis, 9:6955-6961, 2019

PubMed Abstract: Ergothioneine is a thiohistidine derivative with potential benefits on many aging-related diseases. The central step of aerobic ergothioneine biosynthesis is the oxidative C-S bond formation reaction catalyzed by mononuclear nonheme iron sulfoxide synthases (EgtB and Egt1). Thus far, only the EgtB (EgtB ) crystal structure is available, while the structural information for the more industrially attractive Egt1 enzyme is not. Herein, we reported the crystal structure of the ergothioneine sulfoxide synthase (EgtB ) from EgtB has both EgtB- and Egt1-type of activities. Guided by the structural information, we conducted Rosetta Enzyme Design calculations, and we biochemically demonstrated that EgtB can be engineered more toward Egt1-type of activity. This study provides information regarding the factors governing the substrate selectivity in Egt1- and EgtB-catalysis and lays the groundwork for future sulfoxide synthase engineering toward the development of an effective ergothioneine process through a synthetic biology approach.

PubMed: 32257583
DOI: 10.1021/acscatal.9b02054

実験手法

X-RAY DIFFRACTION (2.506 Å)