1AOG

TRYPANOSOMA CRUZI TRYPANOTHIONE REDUCTASE (OXIDIZED FORM)

1AOG の概要

• エントリーDOI: 10.2210/pdb1aog/pdb
• 分子名称: TRYPANOTHIONE REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, MALEIC ACID, ... (4 entities in total)
• 機能のキーワード: trypanothione reductase, fad dependent disulphide oxidoreductase, oxidoreductase
• 由来する生物種: Trypanosoma cruzi
• 細胞内の位置: Cytoplasm: P28593
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 108154.79

構造登録者

Bond, C.S.,Zhang, Y.,Hunter, W.N. (登録日: 1997-07-03, 公開日: 1997-09-17, 最終更新日: 2024-10-23)

主引用文献

Zhang, Y.,Bond, C.S.,Bailey, S.,Cunningham, M.L.,Fairlamb, A.H.,Hunter, W.N.
The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution.
Protein Sci., 5:52-61, 1996

PubMed Abstract: Trypanothione reductase (TR) is an NADPH-dependent flavoprotein unique to protozoan parasites from the genera Trypanosoma and Leishmania and is an important target for the design of improved trypanocidal drugs. We present details of the structure of TR from the human pathogen Trypanosoma cruzi, the agent responsible for Chagas' disease or South American trypanosomiasis. The structure has been solved by molecular replacement, using as the starting model the structure of the enzyme from the nonpathogenic Crithidia fasciculata, and refined to an R-factor of 18.9% for 53,868 reflections with F > or = sigma F between 8.0 and 2.3 A resolution. The model comprises two subunits (968 residues), two FAD prosthetic groups, two maleate ions, and 419 water molecules. The accuracy and geometry of the enzyme model is improved with respect to the C. fasciculata enzyme model. The new structure is described and specific features of the enzyme involved in substrate interactions are compared with previous models of TR and related glutathione reductases from human and Escherichia coli. Structural differences at the edge of the active sites suggest an explanation for the differing specificities toward glutathionylspermidine disulfide.

PubMed: 8771196

実験手法

X-RAY DIFFRACTION (2.3 Å)