› 1y07

X-ray diffraction
1.55Å resolution

Crystal structure of the superoxide reductase from Treponema pallidum

Released:
DOI: 10.2210/pdb1y07/pdb
PDB entry 1y07 coloured by chain, front view.
PDB entry 1y07 coloured by chain, side view.
PDB entry 1y07 coloured by chain, top view.
Source organism: Treponema pallidum subsp. pallidum str. Nichols
Primary publication:
The first crystal structure of class III superoxide reductase from Treponema pallidum.
Santos-Silva T, Trincão J, Carvalho AL, Bonifácio C, Auchère F, Raleiras P, Moura I, Moura JJ, Romão MJ
J Biol Inorg Chem 11 548-58 (2006)
PMID: 16791639

Function and Biology Details

Reaction catalysed: 
Reduced rubredoxin + superoxide + 2 H(+) = oxidized rubredoxin + H(2)O(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-131392 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Desulfoferrodoxin ferrous iron-binding domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 128 amino acids
Theoretical weight: 13.82 KDa
Source organism: Treponema pallidum subsp. pallidum str. Nichols
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O83795 (Residues: 1-128; Coverage: 100%)
Gene name: TP_0823
Sequence domains: Desulfoferrodoxin
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand FE 5 x FE
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2
Unit cell:
a: 119.311Å b: 59.946Å c: 65.52Å
α: 90° β: 104.96° γ: 90°
R-values:
R R work R free
0.189 0.182 0.235
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Enzymatic activity mastered by altering metal coordination spheres.
Moura et al. (2008)
16 other articles

3 mentions without citation

Superoxide dismutases and superoxide reductases.
Sheng et al. (2014)
2 more