2NOX

Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans

2NOX の概要

• エントリーDOI: 10.2210/pdb2nox/pdb
• 分子名称: Tryptophan 2,3-dioxygenase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: helical bundle, heme protein, oxidoreductase
• 由来する生物種: Cupriavidus metallidurans
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 530548.32

構造登録者

Zhang, Y.,Kang, S.A.,Mukherjee, T.,Bale, S.,Crane, B.R.,Begley, T.P.,Ealick, S.E. (登録日: 2006-10-26, 公開日: 2006-12-19, 最終更新日: 2023-08-30)

主引用文献

Zhang, Y.,Kang, S.A.,Mukherjee, T.,Bale, S.,Crane, B.R.,Begley, T.P.,Ealick, S.E.
Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis.
Biochemistry, 46:145-155, 2007

PubMed Abstract: The structure of tryptophan 2,3-dioxygenase (TDO) from Ralstonia metallidurans was determined at 2.4 A. TDO catalyzes the irreversible oxidation of l-tryptophan to N-formyl kynurenine, which is the initial step in tryptophan catabolism. TDO is a heme-containing enzyme and is highly specific for its substrate l-tryptophan. The structure is a tetramer with a heme cofactor bound at each active site. The monomeric fold, as well as the heme binding site, is similar to that of the large domain of indoleamine 2,3-dioxygenase, an enzyme that catalyzes the same reaction except with a broader substrate tolerance. Modeling of the putative (S)-tryptophan hydroperoxide intermediate into the active site, as well as substrate analogue and mutagenesis studies, are consistent with a Criegee mechanism for the reaction.

PubMed: 17198384
DOI: 10.1021/bi0620095

実験手法

X-RAY DIFFRACTION (2.4 Å)