› 7apr

X-ray diffraction
3.1Å resolution

Bacillithiol Disulfide Reductase Bdr (YpdA) from Staphylococcus aureus

Released:
DOI: 10.2210/pdb7apr/pdb
PDB entry 7apr coloured by chain, front view.
PDB entry 7apr coloured by chain, side view.
PDB entry 7apr coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus COL
Primary publication:
The Crystal Structures of Bacillithiol Disulfide Reductase Bdr (YpdA) Provide Structural and Functional Insight into a New Type of FAD-Containing NADPH-Dependent Oxidoreductase.
Hammerstad M, Gudim I, Hersleth HP
OpenAccess logo Biochemistry 59 4793-4798 (2020)
PMID: 33326741

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101608 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyridine nucleotide-disulfide oxidoreductase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 328 amino acids
Theoretical weight: 36.78 KDa
Source organism: Staphylococcus aureus subsp. aureus COL
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2WWS2 (Residues: 1-328; Coverage: 100%)
Gene name: SACOL1520
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase

Ligands and Environments

2 bound ligands:
Ligand FAD 8 x FAD
Ligand NAP 3 x NAP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX IV BEAMLINE BioMAX
Spacegroup: P6122
Unit cell:
a: 180.308Å b: 180.308Å c: 350.459Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.246 0.244 0.291
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Thiol Reductases in Deinococcus Bacteria and Roles in Stress Tolerance.
de Groot et al. (2022)
6 other articles

1 mention without citation

The Crystal Structures of Bacillithiol Disulfide Reductase Bdr (YpdA) Provide Structural and Functional Insight into a New Type of FAD-Containing NADPH-Dependent Oxidoreductase.
Hammerstad et al. (2020)