› 3nq0

X-ray diffraction
2.2Å resolution

Crystal Structure of Tyrosinase from Bacillus megaterium crystallized in the absence of Zinc

Released:
DOI: 10.2210/pdb3nq0/pdb
PDB entry 3nq0 coloured by chain, front view.
PDB entry 3nq0 coloured by chain, side view.
PDB entry 3nq0 coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
First structures of an active bacterial tyrosinase reveal copper plasticity.
Sendovski M, Kanteev M, Ben-Yosef VS, Adir N, Fishman A
J Mol Biol 405 227-37 (2011)
PMID: 21040728

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109772 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosinase copper-binding domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 35.28 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: B2ZB02 (Residues: 1-297; Coverage: 100%)
Sequence domains: Common central domain of tyrosinase
Structure domains: Di-copper center containing domain from catechol oxidase

Ligands and Environments

1 bound ligand:
Ligand CU 2 x CU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 47.82Å b: 78.7Å c: 85.58Å
α: 90° β: 105.29° γ: 90°
R-values:
R R work R free
0.245 0.242 0.292
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme.
Rolff et al. (2011)
18 more

1 mention without citation

Copper active sites in biology.
Solomon et al. (2014)