› 3tue

X-ray diffraction
3Å resolution

The structure of tryparedoxin peroxidase I from Leishmania major

Released:
DOI: 10.2210/pdb3tue/pdb
PDB entry 3tue coloured by chain, front view.
PDB entry 3tue coloured by chain, side view.
PDB entry 3tue coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
The crystal structures of the tryparedoxin-tryparedoxin peroxidase couple unveil the structural determinants of Leishmania detoxification pathway.
Fiorillo A, Colotti G, Boffi A, Baiocco P, Ilari A
PLoS Negl Trop Dis 6 e1781 (2012)
PMID: 22928053

Function and Biology Details

Reaction catalysed: 
Thioredoxin + ROOH = thioredoxin disulfide + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175708 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
thioredoxin-dependent peroxiredoxin Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 219 amino acids
Theoretical weight: 24.33 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4QF76 (Residues: 1-199; Coverage: 100%)
Gene names: LMJF_15_1080, PXN3, TRYP3, TSA, TXNPX
Sequence domains:
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 112.977Å b: 212.385Å c: 90.948Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.233
Expression system: Escherichia coli

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Citations

6 review citations

Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling.
Perkins et al. (2015)
5 more

7 mentions without citation

Recent Advances in Chemotherapeutics for Leishmaniasis: Importance of the Cellular Biochemistry of the Parasite and Its Molecular Interaction with the Host.
Singh et al. (2023)
6 more