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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 lowCrystal structure of Streptomyces tyrosinase in a complex with caddie soaked in a Cu(II)-containing solution for 20 hr: occupancy of Cu(II) is low
Structural highlights
FunctionPublication Abstract from PubMedThe 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 A 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. A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein.,Matoba Y, Bando N, Oda K, Noda M, Higashikawa F, Kumagai T, Sugiyama M J Biol Chem. 2011 Aug 26;286(34):30219-31. Epub 2011 Jul 5. PMID:21730070[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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