2ZMX

Crystal structure of the met1-form of the copper-bound tyrosinase in complex with a caddie protein from Streptomyces castaneoglobisporus obtained by soaking in cupric sulfate solution for 36 hours

Replaces:  1WX3

Summary for 2ZMX

• Entry DOI: 10.2210/pdb2zmx/pdb
• Related: 2ZMY 2ZMZ 2ZN0 2ZN1 2ZN2 2ZN3 2ZN4 2ZN5 2ZN6
• Descriptor: Tyrosinase, CADDIE, COPPER (II) ION, ... (5 entities in total)
• Functional Keywords: tyrosinase, binary complex, type-3 copper, dioxygen, copper transfer, oxidoreductase-metal transport complex, copper, metal-binding, oxidoreductase/metal transport
• Biological source: Streptomyces castaneoglobisporus; More
• Total number of polymer chains: 2
• Total formula weight: 46857.58

Authors

Matoba, Y.,Sugiyama, M. (deposition date: 2008-04-21, release date: 2009-04-07, Last modification date: 2023-11-01)

Primary citation

Matoba, Y.,Kumagai, T.,Yamamoto, A.,Yoshitsu, H.,Sugiyama, M.
Crystallographic Evidence That the Dinuclear Copper Center of Tyrosinase Is Flexible during Catalysis
J.Biol.Chem., 281:8981-8990, 2006

PubMed Abstract: At high resolution, we determined the crystal structures of copper-bound and metal-free tyrosinase in a complex with ORF378 designated as a "caddie" protein because it assists with transportation of two CuII ions into the tyrosinase catalytic center. These structures suggest that the caddie protein covers the hydrophobic molecular surface of tyrosinase and interferes with the binding of a substrate tyrosine to the catalytic site of tyrosinase. The caddie protein, which consists of one six-strandedbeta-sheet and one alpha-helix, has no similarity with all proteins deposited into the Protein Data Bank. Although tyrosinase and catechol oxidase are classified into the type 3 copper protein family, the latter enzyme lacks monooxygenase activity. The difference in catalytic activity is based on the structural observations that a large vacant space is present just above the active center of tyrosinase and that one of the six His ligands for the two copper ions is highly flexible. These structural characteristics of tyrosinase suggest that, in the reaction that catalyzes the ortho-hydroxylation of monophenol, one of the two Cu(II) ions is coordinated by the peroxide-originated oxygen bound to the substrate. Our crystallographic study shows evidence that the tyrosinase active center formed by dinuclear coppers is flexible during catalysis.

PubMed: 16436386
DOI: 10.1074/jbc.M509785200

Experimental method

X-RAY DIFFRACTION (1.33 Å)