› 3e6z

X-ray diffraction
1Å resolution

1.0 A Structure of CusF-W44A-Cu(II) residues 10-88 from Escherichia coli

Released:
DOI: 10.2210/pdb3e6z/pdb
PDB entry 3e6z coloured by chain, front view.
PDB entry 3e6z coloured by chain, side view.
PDB entry 3e6z coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF.
Loftin IR, Blackburn NJ, McEvoy MM
J Biol Inorg Chem 14 905-12 (2009)
PMID: 19381697

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
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: 80 amino acids
Theoretical weight: 8.78 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P77214 (Residues: 32-110; Coverage: 89%)
Gene names: JW0562, b0573, cusF, cusX, ylcC
Sequence domains: Copper binding periplasmic protein CusF
Structure domains: Copper binding periplasmic protein CusF

Ligands and Environments

2 bound ligands:
Ligand CU 1 x CU
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 26.272Å b: 31.615Å c: 84.685Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.214
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The challenges of determining metal-protein affinities.
Xiao et al. (2010)
5 more

5 mentions without citation

Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.
Alav et al. (2021)
4 more