2VUP

Crystal structure of a type II tryparedoxin-dependant peroxidase from Trypanosoma brucei

2VUP の概要

• エントリーDOI: 10.2210/pdb2vup/pdb
• 分子名称: GLUTATHIONE PEROXIDASE-LIKE PROTEIN (2 entities in total)
• 機能のキーワード: oxidoreductase, peroxidase, trypanosoma, trypanothione, dithiol-dependant peroxidase
• 由来する生物種: TRYPANOSOMA BRUCEI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21139.06

構造登録者

Alphey, M.S.,Konig, J.,Fairlamb, A.H. (登録日: 2008-05-28, 公開日: 2008-06-17, 最終更新日: 2023-12-13)

主引用文献

Alphey, M.S.,Konig, J.,Fairlamb, A.H.
Structural and Mechanistic Insights Into Type II Trypanosomatid Tryparedoxin-Dependent Peroxidases.
Biochem.J., 414:375-, 2008

PubMed Abstract: TbTDPX (Trypanosoma brucei tryparedoxin-dependent peroxidase) is a genetically validated drug target in the fight against African sleeping sickness. Despite its similarity to members of the GPX (glutathione peroxidase) family, TbTDPX2 is functional as a monomer, lacks a selenocysteine residue and relies instead on peroxidatic and resolving cysteine residues for catalysis and uses tryparedoxin rather than glutathione as electron donor. Kinetic studies indicate a saturable Ping Pong mechanism, unlike selenium-dependent GPXs, which display infinite K(m) and V(max) values. The structure of the reduced enzyme at 2.1 A (0.21 nm) resolution reveals that the catalytic thiol groups are widely separated [19 A (0.19 nm)] and thus unable to form a disulphide bond without a large conformational change in the secondary-structure architecture, as reported for certain plant GPXs. A model of the oxidized enzyme structure is presented and the implications for small-molecule inhibition are discussed.

PubMed: 18522537
DOI: 10.1042/BJ20080889

実験手法

X-RAY DIFFRACTION (2.1 Å)