› 1zeq

X-ray diffraction
1.5Å resolution

1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli

Released:
DOI: 10.2210/pdb1zeq/pdb
PDB entry 1zeq coloured by chain, front view.
PDB entry 1zeq coloured by chain, side view.
PDB entry 1zeq coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A novel copper-binding fold for the periplasmic copper resistance protein CusF.
Loftin IR, Franke S, Roberts SA, Weichsel A, Héroux A, Montfort WR, Rensing C, McEvoy MM
Biochemistry 44 10533-40 (2005)
PMID: 16060662

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160134 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cation efflux system protein CusF Chain: X
Molecule details ›
Chain: X
Length: 84 amino acids
Theoretical weight: 9.34 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P77214 (Residues: 28-110; Coverage: 93%)
Gene names: JW0562, b0573, cusF, cusX, ylcC
Sequence domains: Copper binding periplasmic protein CusF
Structure domains: Copper binding periplasmic protein CusF

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P212121
Unit cell:
a: 39.3Å b: 39.326Å c: 43.693Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.207
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

Copper metallochaperones.
Robinson et al. (2010)
16 more

15 mentions without citation

Structural biology of copper trafficking.
Boal et al. (2009)
14 more