› 6hk5

X-ray diffraction
2.04Å resolution

X-ray structure of a truncated mutant of the metallochaperone CooJ with a high-affinity nickel-binding site

Released:
DOI: 10.2210/pdb6hk5/pdb
PDB entry 6hk5 coloured by chain, front view.
PDB entry 6hk5 coloured by chain, side view.
PDB entry 6hk5 coloured by chain, top view.
Source organism: Rhodospirillum rubrum
Primary publication:
The carbon monoxide dehydrogenase accessory protein CooJ is a histidine-rich multidomain dimer containing an unexpected Ni(II)-binding site.
Alfano M, Pérard J, Carpentier P, Basset C, Zambelli B, Timm J, Crouzy S, Ciurli S, Cavazza C
J Biol Chem 294 7601-7614 (2019)
PMID: 30858174

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-159840 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CooJ Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 68 amino acids
Theoretical weight: 7.61 KDa
Source organism: Rhodospirillum rubrum
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P72321 (Residues: 1-68; Coverage: 59%)
Gene name: cooJ

Ligands and Environments

6 bound ligands:
Ligand NI 4 x NI
Ligand PEG 4 x PEG
Ligand CL 3 x CL
Ligand CA 1 x CA
Ligand PGE 1 x PGE
Ligand Z3P 1 x Z3P
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: P21
Unit cell:
a: 46.8Å b: 74.28Å c: 70.64Å
α: 90° β: 92.74° γ: 90°
R-values:
R R work R free
0.202 0.2 0.258
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

1 review citation

Structure, function, and biosynthesis of nickel-dependent enzymes.
Alfano et al. (2020)
4 other articles

1 mention without citation

The carbon monoxide dehydrogenase accessory protein CooJ is a histidine-rich multidomain dimer containing an unexpected Ni(II)-binding site.
Alfano et al. (2019)