4X8B
Ergothioneine-biosynthetic sulfoxide synthase EgtB, apo form
4X8B の概要
エントリーDOI | 10.2210/pdb4x8b/pdb |
分子名称 | Sulfoxide synthase EgtB, GLYCEROL, CHLORIDE ION, ... (7 entities in total) |
機能のキーワード | 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 | 100357.45 |
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: 2017-09-06) |
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 Cited by 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: 25597398DOI: 10.1002/anie.201410045 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.7 Å) |
構造検証レポート
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