Publication Date:
2015-08-25
Description:
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 ofStreptomyces griseoflavusAc-993, expressed inEscherichia coliand purified to homogeneity. The crystals of SgfSL belonged to the monoclinic space groupP21, with unit-cell parametersa= 74.64,b= 94.72,c= 117.40 Å, β = 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 Å3 Da−1according to the monomer molecular weight of 35.6 kDa.
Electronic ISSN:
2053-230X
Topics:
Biology
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Chemistry and Pharmacology
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Geosciences
,
Physics
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