Literature DB >> 20823537

Crystallization and preliminary X-ray crystallographic analysis of a bacterial tyrosinase from Bacillus megaterium.

Mor Sendovski1, Margarita Kanteev, Vered Shuster Ben-Yosef, Noam Adir, Ayelet Fishman.   

Abstract

Tyrosinases are type 3 copper enzymes that are involved in the production of melanin and have two copper ions in the active site. Here, the crystallization and primary analysis of a tyrosinase from Bacillus megaterium is reported. The purified protein was crystallized in the absence or presence of zinc ions and the crystals diffracted to a resolution of 2.0 A. Crystals obtained in the presence of zinc belonged to space group P2(1)2(1)2(1), while crystals grown in the absence of zinc belonged to space group P2(1). In both space groups the asymmetric unit contained a dimer, with minor differences in the crystal density and in packing interactions.

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Year:  2010        PMID: 20823537      PMCID: PMC2935238          DOI: 10.1107/S1744309110031520

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  21 in total

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  7 in total

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3.  The mechanism of copper uptake by tyrosinase from Bacillus megaterium.

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  7 in total

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