1wxc

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spinqualitylabelsall models 1wxc, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of the copper-free Streptomyces castaneoglobisporus tyrosinase complexed with a caddie protein

Overview

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.

About this Structure

1WXC is a Protein complex structure of sequences from Streptomyces castaneoglobisporus with NO3 as ligand. Active as Monophenol monooxygenase, with EC number 1.14.18.1 Full crystallographic information is available from OCA.

Reference

Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis., Matoba Y, Kumagai T, Yamamoto A, Yoshitsu H, Sugiyama M, J Biol Chem. 2006 Mar 31;281(13):8981-90. Epub 2006 Jan 25. PMID:16436386

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