› 3awv

X-ray diffraction
1.4Å resolution

Crystal structure of Streptomyces tyrosinase in a complex with caddie soaked in a Cu(II)-containing solution for 80 hr: occupancy of CuA is low

Released:
DOI: 10.2210/pdb3awv/pdb
PDB entry 3awv coloured by chain, front view.
PDB entry 3awv coloured by chain, side view.
PDB entry 3awv coloured by chain, top view.
Source organism: Streptomyces castaneoglobisporus
Primary publication:
A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein.
Matoba Y, Bando N, Oda K, Noda M, Higashikawa F, Kumagai T, Sugiyama M
J Biol Chem 286 30219-31 (2011)
PMID: 21730070

Function and Biology Details

Reaction catalysed: 
(1a) L-tyrosine + 1/2 O(2) = L-dopa
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182976 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosinase copper-binding domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 281 amino acids
Theoretical weight: 32.09 KDa
Source organism: Streptomyces castaneoglobisporus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q83WS2 (Residues: 1-273; Coverage: 100%)
Sequence domains: Common central domain of tyrosinase
Structure domains: Di-copper center containing domain from catechol oxidase
MelC Chain: B
Molecule details ›
Chain: B
Length: 134 amino acids
Theoretical weight: 14.09 KDa
Source organism: Streptomyces castaneoglobisporus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q83WS1 (Residues: 1-126; Coverage: 100%)
Sequence domains: Tyrosinase co-factor MelC1
Structure domains: protein ne1242 domain like

Ligands and Environments

2 bound ligands:
Ligand CU 3 x CU
Ligand NO3 6 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P21212
Unit cell:
a: 65.09Å b: 97.85Å c: 55.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.218
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Diverse immune functions of hemocyanins.
Coates et al. (2014)
5 more

1 mention without citation

A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein.
Matoba et al. (2011)