› 1moj

X-ray diffraction
1.9Å resolution

Crystal structure of an archaeal dps-homologue from Halobacterium salinarum

Released:
DOI: 10.2210/pdb1moj/pdb
PDB entry 1moj coloured by chain, front view.
PDB entry 1moj coloured by chain, side view.
PDB entry 1moj coloured by chain, top view.
Source organism: Halobacterium salinarum
Primary publication:
Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states.
Zeth K, Offermann S, Essen LO, Oesterhelt D
Proc Natl Acad Sci U S A 101 13780-5 (2004)
PMID: 15365182

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190907 (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: 182 amino acids
Theoretical weight: 20.12 KDa
Source organism: Halobacterium salinarum
UniProt:
  • Canonical: Q9HMP7 (Residues: 1-182; Coverage: 100%)
Gene names: OE4427R, VNG_2443G, dps, dpsA
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

3 bound ligands:
Ligand FE 6 x FE
Ligand NA 2 x NA
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P321
Unit cell:
a: 90.747Å b: 90.747Å c: 149.41Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.147 0.182

Quick links

Citations

9 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)
8 more

1 mention without citation

Salt-bridge energetics in halophilic proteins.
Nayek et al. (2014)