4hd6

Crystal Structure of Tyrosinase from Bacillus megaterium V218F mutant soaked in CuSO4

spinqualitylabelsall models 4hd6, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hd6 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. Ligands: CU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B2ZB02_PRIMG Publication Abstract from PubMed Tyrosinase is a type 3 copper enzyme with great potential for production of commercially valuable diphenols from monophenols. However, the use of tyrosinase is limited by its further oxidation of diphenols to quinones. We recently determined the structure of the Bacillus megaterium tyrosinase revealing a residue, V218, which we proposed to take part in positioning of substrates within the active site. In the structure of catechol oxidase from Ipomoea batatas, the lack of monophenolase activity was attributed to the presence of F261 near CuA. Consequently, we engineered two variants, V218F and V218G. V218F was expected to have a decreased monophenolase activity, due to the bulky residue extending into the active site. Surprisingly, both V218F and V218G exhibited a 9- and 4.4-fold higher monophenolase/diphenolase activity ratio, respectively. X-ray structures of variant V218F display a flexibility of the phenylalanine residue along with an adjacent histidine, which we propose to be the source of the change in activity ratio. Influencing the monophenolase/diphenolase activity ratio in tyrosinase.,Goldfeder M, Kanteev M, Adir N, Fishman A Biochim Biophys Acta. 2013 Jan 8. pii: S1570-9639(13)00003-4. doi:, 10.1016/j.bbapap.2012.12.021. PMID:23305929 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosinase 3D structures

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