1AOG

TRYPANOSOMA CRUZI TRYPANOTHIONE REDUCTASE (OXIDIZED FORM)

Summary for 1AOG

• Entry DOI: 10.2210/pdb1aog/pdb
• Descriptor: TRYPANOTHIONE REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, MALEIC ACID, ... (4 entities in total)
• Functional Keywords: trypanothione reductase, fad dependent disulphide oxidoreductase, oxidoreductase
• Biological source: Trypanosoma cruzi
• Cellular location: Cytoplasm: P28593
• Total number of polymer chains: 2
• Total formula weight: 108154.79

Authors

Bond, C.S.,Zhang, Y.,Hunter, W.N. (deposition date: 1997-07-03, release date: 1997-09-17, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)