3AWT

Crystal structure of Streptomyces tyrosinase in a complex with caddie soaked in a Cu(II)-containing solution for 20 hr: occupancy of Cu(II) is high

Summary for 3AWT

• Entry DOI: 10.2210/pdb3awt/pdb
• Related: 3AWS 3AWU 3AWV 3AWW 3AWX 3AWY 3AWZ 3AX0
• Descriptor: Tyrosinase, MelC, COPPER (II) ION, ... (5 entities in total)
• Functional Keywords: tyrosinase, binary complex, type-3 copper, dioxygen, copper transfer, oxidoreductase-metal transport complex, oxidoreductase/metal transport
• Biological source: Streptomyces castaneoglobisporus; More
• Total number of polymer chains: 2
• Total formula weight: 46805.42

Authors

Matoba, Y.,Sugiyama, M. (deposition date: 2011-03-26, release date: 2011-06-29, Last modification date: 2023-11-01)

Primary citation

Matoba, Y.,Bando, N.,Oda, K.,Noda, M.,Higashikawa, F.,Kumagai, T.,Sugiyama, M.
A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein
J.Biol.Chem., 286:30219-30231, 2011

PubMed Abstract: The Cu(II)-soaked crystal structure of tyrosinase that is present in a complex with a protein, designated "caddie," which we previously determined, possesses two copper ions at its catalytic center. We had identified two copper-binding sites in the caddie protein and speculated that copper bound to caddie may be transported to the tyrosinase catalytic center. In our present study, at a 1.16-1.58 Å resolution, we determined the crystal structures of tyrosinase complexed with caddie prepared by altering the soaking time of the copper ion and the structures of tyrosinase complexed with different caddie mutants that display little or no capacity to activate tyrosinase. Based on these structures, we propose a molecular mechanism by which two copper ions are transported to the tyrosinase catalytic center with the assistance of caddie acting as a metallochaperone.

PubMed: 21730070
DOI: 10.1074/jbc.M111.256818

Experimental method

X-RAY DIFFRACTION (1.35 Å)