4ZFL

Ergothioneine-biosynthetic Ntn hydrolase variant EgtC_C2A with natural substrate

4ZFL の概要

• エントリーDOI: 10.2210/pdb4zfl/pdb
• 関連するPDBエントリー: 4ZFJ 4ZFK
• 分子名称: Amidohydrolase EgtC, (1S)-1-carboxy-4-({(1R)-1-carboxy-2-[(S)-{4-[(2S)-2-carboxy-2-(trimethylammonio)ethyl]-1H-imidazol-2-yl}sulfinyl]ethyl}amino)-4-oxobutan-1-aminium, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: ntn hydrolase, ergothioneine biosynthesis, sulfur chemistry, mycobacteria, hydrolase
• 由来する生物種: Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 306856.74

構造登録者

Vit, A.,Seebeck, F.P.,Blankenfeldt, W. (登録日: 2015-04-21, 公開日: 2015-07-01, 最終更新日: 2024-01-10)

主引用文献

Vit, A.,Mashabela, G.T.,Blankenfeldt, W.,Seebeck, F.P.
Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC.
Chembiochem, 16:1490-1496, 2015

PubMed Abstract: The ubiquitous sulfur metabolite ergothioneine is biosynthesized by oxidative attachment of a sulfur atom to the imidazole ring of Nα-trimethylhistidine. Most actinobacteria, including Mycobacterium tuberculosis, use γ-glutamyl cysteine as a sulfur donor. In subsequent steps the carbon scaffold of γ-glutamyl cysteine is removed by the glutamine amidohydrolase EgtC and the β-lyase EgtE. We determined the crystal structure of EgtC from Mycobacterium smegmatis in complex with its physiological substrate. The set of active site residues that define substrate specificity in EgtC are highly conserved, even in homologues that are not involved in ergothioneine production. This conservation is compounded by the phylogenetic distribution of EgtC-like enzymes indicates that their last common ancestor might have emerged for a purpose other than ergothioneine production.

PubMed: 26079795
DOI: 10.1002/cbic.201500168

実験手法

X-RAY DIFFRACTION (1.7 Å)