› 3rfu

X-ray diffraction
3.2Å resolution

Crystal structure of a copper-transporting PIB-type ATPase

Released:
DOI: 10.2210/pdb3rfu/pdb
PDB entry 3rfu coloured by chain, front view.
PDB entry 3rfu coloured by chain, side view.
PDB entry 3rfu coloured by chain, top view.
Source organism: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Primary publication:
Crystal structure of a copper-transporting PIB-type ATPase.
Gourdon P, Liu XY, Skjørringe T, Morth JP, Møller LB, Pedersen BP, Nissen P
Nature 475 59-64 (2011)
PMID: 21716286

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178686 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-exporting P-type ATPase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 736 amino acids
Theoretical weight: 78.33 KDa
Source organism: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5ZWR1 (Residues: 1-736; Coverage: 100%)
Gene names: copA, lpg1024
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ALF 4 x ALF
Ligand MG 4 x MG
Ligand K 4 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA, BESSY BEAMLINE 14.1
Spacegroup: P1
Unit cell:
a: 44.15Å b: 72.98Å c: 329.95Å
α: 89.96° β: 90.04° γ: 90.22°
R-values:
R R work R free
0.236 0.235 0.261
Expression system: Escherichia coli

Quick links

Citations

45 review citations

Copper toxicity and the origin of bacterial resistance--new insights and applications.
Dupont et al. (2011)
44 more

33 mentions without citation

Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
Argüello et al. (2011)
32 more