› 3nsy

X-ray diffraction
2.1Å resolution

The multi-copper oxidase CueO with six Met to Ser mutations (M358S,M361S,M362S,M364S,M366S,M368S)

Released:
DOI: 10.2210/pdb3nsy/pdb
PDB entry 3nsy coloured by chain, front view.
PDB entry 3nsy coloured by chain, side view.
PDB entry 3nsy coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I): functional role of a methionine-rich sequence.
Singh SK, Roberts SA, McDevitt SF, Weichsel A, Wildner GF, Grass GB, Rensing C, Montfort WR
J Biol Chem 286 37849-57 (2011)
PMID: 21903583

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-153204 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multicopper oxidase CueO Chain: A
Molecule details ›
Chain: A
Length: 511 amino acids
Theoretical weight: 55.75 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36649 (Residues: 29-516; Coverage: 100%)
Gene names: JW0119, b0123, cueO, yacK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

2 bound ligands:
Ligand CU 4 x CU
Ligand C2O 1 x C2O
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 50.052Å b: 91.259Å c: 53.979Å
α: 90° β: 102.34° γ: 90°
R-values:
R R work R free
0.173 0.17 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Copper homeostasis at the host-pathogen interface.
Hodgkinson et al. (2012)
8 more

1 mention without citation

Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I): functional role of a methionine-rich sequence.
Singh et al. (2011)