5ce9 | pdb_00005ce9

structure of tyrosinase from walnut (Juglans regia)

spinqualitylabelsall models 5ce9, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ce9 is a 2 chain structure with sequence from Juglans regia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU, NA, O Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed Tyrosinases and catechol oxidases are members of the class of type III copper enzymes. While tyrosinases accept both mono- and o-diphenols as substrates, only the latter substrate is converted by catechol oxidases. Researchers have been working for decades to elucidate the monophenolase/diphenolase specificity on a structural level and have introduced an early hypothesis that states that the reason for the lack of monophenolase activity in catechol oxidases may be its structurally restricted active site. However, recent structural and biochemical studies of this enzyme class have raised doubts about this theory. Herein, the first crystal structure of a plant tyrosinase (from Juglans regia) is presented. The structure reveals that the distinction between mono- and diphenolase activity does not depend on the degree of restriction of the active site, and thus a more important role for amino acid residues located at the entrance to and in the second shell of the active site is proposed. The Structure of a Plant Tyrosinase from Walnut Leaves Reveals the Importance of "Substrate-Guiding Residues" for Enzymatic Specificity.,Bijelic A, Pretzler M, Molitor C, Zekiri F, Rompel A Angew Chem Int Ed Engl. 2015 Oct 16. doi: 10.1002/anie.201506994. PMID:26473311 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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