› 2wba

X-ray diffraction
2.3Å resolution

Properties of Trypanothione Reductase From T. brucei

Released:
DOI: 10.2210/pdb2wba/pdb
PDB entry 2wba coloured by chain, front view.
PDB entry 2wba coloured by chain, side view.
PDB entry 2wba coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Comparative structural, kinetic and inhibitor studies of Trypanosoma brucei trypanothione reductase with T. cruzi.
Jones DC, Ariza A, Chow WH, Oza SL, Fairlamb AH
Mol Biochem Parasitol 169 12-9 (2010)
PMID: 19747949

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153811 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypanothione reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 492 amino acids
Theoretical weight: 53.22 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39051 (Residues: 1-492; Coverage: 100%)
Gene name: TPR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP

Cofactor: Ligand FAD 2 x FAD
3 bound ligands:
Ligand GOL 8 x GOL
Ligand PG4 1 x PG4
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 63.63Å b: 132.713Å c: 161.287Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.227
Expression system: Escherichia coli BL21(DE3)

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Citations

7 review citations

Low-molecular-mass antioxidants in parasites.
Krauth-Siegel et al. (2012)
6 more

5 mentions without citation

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