› 3e5q

X-ray diffraction
3.2Å resolution

Unbound Oxidised CprK

Released:
DOI: 10.2210/pdb3e5q/pdb
PDB entry 3e5q coloured by chain, front view.
PDB entry 3e5q coloured by chain, side view.
PDB entry 3e5q coloured by chain, top view.
Source organism: Desulfitobacterium hafniense DCB-2
Primary publication:
Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator.
Levy C, Pike K, Heyes DJ, Joyce MG, Gabor K, Smidt H, van der Oost J, Leys D
Mol Microbiol 70 151-67 (2008)
PMID: 18717788

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110699 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclic nucleotide-binding protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 250 amino acids
Theoretical weight: 28.4 KDa
Source organism: Desulfitobacterium hafniense DCB-2
Expression system: Escherichia coli
UniProt:
  • Canonical: B8FW11 (Residues: 1-232; Coverage: 100%)
Gene name: Dhaf_0733
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 79.405Å b: 64.71Å c: 148.355Å
α: 90° β: 105.29° γ: 90°
R-values:
R R work R free
0.261 0.258 0.318
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Thiol-based redox switches and gene regulation.
Antelmann et al. (2011)
8 more

2 mentions without citation

Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator.
Levy et al. (2008)
1 more