› 1n1q

X-ray diffraction
2.2Å resolution

Crystal structure of a Dps protein from Bacillus brevis

Released:
DOI: 10.2210/pdb1n1q/pdb
PDB entry 1n1q coloured by chain, front view.
PDB entry 1n1q coloured by chain, side view.
PDB entry 1n1q coloured by chain, top view.
Source organism: Brevibacillus brevis
Primary publication:
The multi-layered structure of Dps with a novel di-nuclear ferroxidase center.
Ren B, Tibbelin G, Kajino T, Asami O, Ladenstein R
J Mol Biol 329 467-77 (2003)
PMID: 12767829

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dodecamer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160725 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA protection during starvation protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 149 amino acids
Theoretical weight: 16.34 KDa
Source organism: Brevibacillus brevis
UniProt:
  • Canonical: P83695 (Residues: 1-149; Coverage: 100%)
Gene name: dps
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

1 bound ligand:
Ligand FEO 4 x FEO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R3
Unit cell:
a: 86.911Å b: 86.911Å c: 220.808Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.208

Quick links

Citations

10 review citations

Structure, function and regulation of the DNA-binding protein Dps and its role in acid and oxidative stress resistance in Escherichia coli: a review.
Calhoun et al. (2011)
9 more

2 mentions without citation

DNA Charge Transport: from Chemical Principles to the Cell.
Arnold et al. (2016)
1 more