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Crystallization and X-ray diffraction studies of a two-domain laccase from Streptomyces griseoflavus.

ABSTRACT: Laccase (EC 1.10.3.2) is one of the most common copper-containing oxidases; it is found in many organisms and catalyzes the oxidation of primarily phenolic compounds by oxygen. Two-domain laccases have unusual thermostability, resistance to inhibitors and an alkaline optimum of activity. The causes of these properties in two-domain laccases are poorly understood. A recombinant two-domain laccase (SgfSL) was cloned from the genome of Streptomyces griseoflavus Ac-993, expressed in Escherichia coli and purified to homogeneity. The crystals of SgfSL belonged to the monoclinic space group P21, with unit-cell parameters a = 74.64, b = 94.72, c = 117.40?Å, ? = 90.672°, and diffraction data were collected to 2.0?Å resolution using a synchrotron-radiation source. Two functional trimers per asymmetric unit correspond to a Matthews coefficient of 1.99?Å(3)?Da(-1) according to the monomer molecular weight of 35.6?kDa.

SUBMITTER: Tishchenko S 

PROVIDER: S-EPMC4555929 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature

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Crystallization and X-ray diffraction studies of a two-domain laccase from Streptomyces griseoflavus.

Tishchenko Svetlana S   Gabdulkhakov Azat A   Trubitsina Liubov L   Lisov Alexander A   Zakharova Marina M   Leontievsky Alexey A  

Acta crystallographica. Section F, Structural biology communications 20150825 Pt 9

Laccase (EC 1.10.3.2) is one of the most common copper-containing oxidases; it is found in many organisms and catalyzes the oxidation of primarily phenolic compounds by oxygen. Two-domain laccases have unusual thermostability, resistance to inhibitors and an alkaline optimum of activity. The causes of these properties in two-domain laccases are poorly understood. A recombinant two-domain laccase (SgfSL) was cloned from the genome of Streptomyces griseoflavus Ac-993, expressed in Escherichia coli  ...[more]

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