2zwe

Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 40 minutes

spinqualitylabelsall models 2zwe, resolution 1.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zwe is a 2 chain structure with sequence from Streptomyces castaneoglobisporus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU, NO3 NonStd Res: DAH Related: 1wxc, 1wx2, 2zmx, 2zmy, 2zmz, 2zwc, 2zwd, 2zwf, 2zwg Gene: TYRC (Streptomyces castaneoglobisporus), ORF378 (Streptomyces castaneoglobisporus) Activity: Monophenol monooxygenase, with EC number 1.14.18.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosinase

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