› 2ux1

X-ray diffraction
1.8Å resolution

Identification of two zinc-binding sites in the Streptococcus suis Dpr protein

Released:
DOI: 10.2210/pdb2ux1/pdb
PDB entry 2ux1 coloured by chain, front view.
PDB entry 2ux1 coloured by chain, side view.
PDB entry 2ux1 coloured by chain, top view.
Source organism: Streptococcus suis
Primary publication:
Structural basis of the zinc- and terbium-mediated inhibition of ferroxidase activity in Dps ferritin-like proteins.
Havukainen H, Haataja S, Kauko A, Pulliainen AT, Salminen A, Haikarainen T, Finne J, Papageorgiou AC
Protein Sci 17 1513-21 (2008)
PMID: 18552126

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-143200 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA protection during starvation protein Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 165 amino acids
Theoretical weight: 18.57 KDa
Source organism: Streptococcus suis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CB53 (Residues: 8-172; Coverage: 96%)
Gene names: dpr, dps
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

4 bound ligands:
Ligand ZN 24 x ZN
Ligand CA 4 x CA
Ligand EPE 4 x EPE
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 104.52Å b: 137.69Å c: 142.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.248
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Dps-like proteins: structural and functional insights into a versatile protein family.
Haikarainen et al. (2010)
3 more

1 mention without citation

Structural basis of the zinc- and terbium-mediated inhibition of ferroxidase activity in Dps ferritin-like proteins.
Havukainen et al. (2008)