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Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1200-4. doi: 10.1107/S2053230X15014375. Epub 2015 Aug 25.

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

Author information

1
Institute of Protein Research, Federal Agency of Scientific Organization, Institutskaya 4, 142290 Pushchino, Moscow Region, Russian Federation.
2
G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Federal Agency of Scientific Organization, Prospect Nauki 5, 142290 Pushchino, Moscow Region, Russian Federation.

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, 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 Å(3) Da(-1) according to the monomer molecular weight of 35.6 kDa.

KEYWORDS:

Streptomyces griseoflavus; two-domain laccase

PMID:
26323308
PMCID:
PMC4555929
DOI:
10.1107/S2053230X15014375
[Indexed for MEDLINE]
Free PMC Article

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