› 1nda

X-ray diffraction
3.3Å resolution

THE STRUCTURE OF TRYPANOSOMA CRUZI TRYPANOTHIONE REDUCTASE IN THE OXIDIZED AND NADPH REDUCED STATE

Released:
DOI: 10.2210/pdb1nda/pdb
PDB entry 1nda coloured by chain, front view.
PDB entry 1nda coloured by chain, side view.
PDB entry 1nda coloured by chain, top view.
Source organism: Trypanosoma cruzi
Primary publication:
The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state.
Lantwin CB, Schlichting I, Kabsch W, Pai EF, Krauth-Siegel RL
Proteins 18 161-73 (1994)
PMID: 8159665

Function and Biology Details

Reaction catalysed: 
Trypanothione + NADP(+) = trypanothione disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151248 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypanothione reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 491 amino acids
Theoretical weight: 53.8 KDa
Source organism: Trypanosoma cruzi
Expression system: Not provided
UniProt:
  • Canonical: P28593 (Residues: 2-492; Coverage: 100%)
Gene name: TPR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 136.3Å b: 91.1Å c: 126Å
α: 90° β: 94° γ: 90°
R-values:
R R work R free
0.206 0.206 not available
Expression system: Not provided

Quick links

Citations

5 review citations

Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia.
Krauth-Siegel et al. (2005)
4 more

2 mentions without citation

Polyamines in protozoan pathogens.
Phillips MA. (2018)
1 more