2NW7

Crystal Structure of Tryptophan 2,3-dioxygenase (TDO) from Xanthomonas campestris in complex with ferric heme. Northeast Structural Genomics Target XcR13

2NW7 の概要

• エントリーDOI: 10.2210/pdb2nw7/pdb
• 関連するPDBエントリー: 1YW0 1ZEE 2NW8 2NW9 2NWB
• 分子名称: Tryptophan 2,3-dioxygenase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: all alpha-helical protein, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, oxidoreductase
• 由来する生物種: Xanthomonas campestris pv. campestris
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 145391.64

構造登録者

Forouhar, F.,Anderson, J.L.R.,Mowat, C.G.,Hussain, A.,Bruckmann, C.,Thackray, S.J.,Seetharaman, J.,Tucker, T.,Ho, C.K.,Ma, L.C.,Cunningham, K.,Janjua, H.,Zhao, L.,Xiao, R.,Liu, J.,Baran, M.C.,Acton, T.B.,Rost, B.,Montelione, G.T.,Chapman, S.K.,Tong, L.,Northeast Structural Genomics Consortium (NESG) (登録日: 2006-11-14, 公開日: 2006-12-19, 最終更新日: 2023-08-30)

主引用文献

Forouhar, F.,Anderson, J.L.,Mowat, C.G.,Vorobiev, S.M.,Hussain, A.,Abashidze, M.,Bruckmann, C.,Thackray, S.J.,Seetharaman, J.,Tucker, T.,Xiao, R.,Ma, L.C.,Zhao, L.,Acton, T.B.,Montelione, G.T.,Chapman, S.K.,Tong, L.
Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
Proc.Natl.Acad.Sci.Usa, 104:473-478, 2007

PubMed Abstract: Tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) constitute an important, yet relatively poorly understood, family of heme-containing enzymes. Here, we report extensive structural and biochemical studies of the Xanthomonas campestris TDO and a related protein SO4414 from Shewanella oneidensis, including the structure at 1.6-A resolution of the catalytically active, ferrous form of TDO in a binary complex with the substrate L-Trp. The carboxylate and ammonium moieties of tryptophan are recognized by electrostatic and hydrogen-bonding interactions with the enzyme and a propionate group of the heme, thus defining the L-stereospecificity. A second, possibly allosteric, L-Trp-binding site is present at the tetramer interface. The sixth coordination site of the heme-iron is vacant, providing a dioxygen-binding site that would also involve interactions with the ammonium moiety of L-Trp and the amide nitrogen of a glycine residue. The indole ring is positioned correctly for oxygenation at the C2 and C3 atoms. The active site is fully formed only in the binary complex, and biochemical experiments confirm this induced-fit behavior of the enzyme. The active site is completely devoid of water during catalysis, which is supported by our electrochemical studies showing significant stabilization of the enzyme upon substrate binding.

PubMed: 17197414
DOI: 10.1073/pnas.0610007104

実験手法

X-RAY DIFFRACTION (2.7 Å)