7P46

Crystal Structure of Xanthomonas campestris Tryptophan 2,3-dioxygenase (TDO)

7P46 の概要

• エントリーDOI: 10.2210/pdb7p46/pdb
• 分子名称: Tryptophan 2,3-dioxygenase, PROTOPORPHYRIN IX CONTAINING FE, CYANIDE ION, ... (7 entities in total)
• 機能のキーワード: dioxygenase, cyanide, kynurenine, oxidoreductase
• 由来する生物種: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 273215.48

構造登録者

Kwon, H.,Basran, J.,Booth, E.S.,Campbell, L.P.,Thackray, S.J.,Moody, P.C.E.,Mowat, C.G.,Raven, E.L. (登録日: 2021-07-09, 公開日: 2021-10-06, 最終更新日: 2024-01-31)

主引用文献

Basran, J.,Booth, E.S.,Campbell, L.P.,Thackray, S.J.,Jesani, M.H.,Clayden, J.,Moody, P.C.E.,Mowat, C.G.,Kwon, H.,Raven, E.L.
Binding of l-kynurenine to X. campestris tryptophan 2,3-dioxygenase.
J.Inorg.Biochem., 225:111604-111604, 2021

PubMed Abstract: The kynurenine pathway is the major route of tryptophan metabolism. The first step of this pathway is catalysed by one of two heme-dependent dioxygenase enzymes - tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) - leading initially to the formation of N-formylkynurenine (NFK). In this paper, we present a crystal structure of a bacterial TDO from X. campestris in complex with l-kynurenine, the hydrolysed product of NFK. l-kynurenine is bound at the active site in a similar location to the substrate (l-Trp). Hydrogen bonding interactions with Arg117 and the heme 7-propionate anchor the l-kynurenine molecule into the pocket. A mechanism for the hydrolysis of NFK in the active site is presented.

PubMed: 34571402
DOI: 10.1016/j.jinorgbio.2021.111604

実験手法

X-RAY DIFFRACTION (1.7 Å)