4PW8

Human tryptophan 2,3-dioxygenase

4PW8 の概要

• エントリーDOI: 10.2210/pdb4pw8/pdb
• 分子名称: Tryptophan 2,3-dioxygenase, COBALT (II) ION (3 entities in total)
• 機能のキーワード: dioxygenase, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 353173.34

構造登録者

Meng, B.,Wu, D.,Gu, J.H.,Ouyang, S.Y.,Ding, W.,Liu, Z.J. (登録日: 2014-03-19, 公開日: 2014-08-06, 最終更新日: 2023-11-08)

主引用文献

Meng, B.,Wu, D.,Gu, J.,Ouyang, S.,Ding, W.,Liu, Z.J.
Structural and functional analyses of human tryptophan 2,3-dioxygenase
Proteins, 82:3210-3216, 2014

PubMed Abstract: Tryptophan 2,3-dioxygenase (TDO), one of the two key enzymes in the kynurenine pathway, catalyzes the indole ring cleavage at the C2-C3 bond of L-tryptophan. This is a rate-limiting step in the regulation of tryptophan concentration in vivo, and is thus important in drug discovery for cancer and immune diseases. Here, we report the crystal structure of human TDO (hTDO) without the heme cofactor to 2.90 Å resolution. The overall fold and the tertiary assembly of hTDO into a tetramer, as well as the active site architecture, are well conserved and similar to the structures of known orthologues. Kinetic and mutational studies confirmed that eight residues play critical roles in L-tryptophan oxidation.

PubMed: 25066423
DOI: 10.1002/prot.24653

実験手法

X-RAY DIFFRACTION (2.902 Å)