4p6s

Crystal Structure of tyrosinase from Bacillus megaterium with L-DOPA in the active site

spinqualitylabelsall models 4p6s, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4p6s is a 2 chain structure with sequence from Priestia megaterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: DAH, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B2ZB02_PRIMG Publication Abstract from PubMed Tyrosinase is responsible for the two initial enzymatic steps in the conversion of tyrosine to melanin. Many tyrosinase mutations are the leading cause of albinism in humans, and it is a prominent biotechnology and pharmaceutical industry target. Here we present crystal structures that show that both monophenol hydroxylation and diphenol oxidation occur at the same site. It is suggested that concurrent presence of a phenylalanine above the active site and a restricting thioether bond on the histidine coordinating CuA prevent hydroxylation of monophenols by catechol oxidases. Furthermore, a conserved water molecule activated by E195 and N205 is proposed to mediate deprotonation of the monophenol at the active site. Overall, the structures reveal precise steps in the enzymatic catalytic cycle as well as differences between tyrosinases and other type-3 copper enzymes. Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins.,Goldfeder M, Kanteev M, Isaschar-Ovdat S, Adir N, Fishman A Nat Commun. 2014 Jul 30;5:4505. doi: 10.1038/ncomms5505. PMID:25074014 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosinase 3D structures

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