Purification, crystallisation and X-ray diffraction study of fully functional laccases from two ligninolytic fungi.
Laccase isozymes from the white-rot basidiomycete fungi Trametes versicolor and Pycnoporus cinnabarinus were purified to apparent iso-electric homogeneity and crystallised. T. versicolor laccase crystallises in two crystal forms, both with the orthorhombic space group P2(1)2(1)2(1), which diffract to 1.9 and 2.95 A resolution, respectively. The crystals of P. cinnabarinus laccase belong to the monoclinic space group C2 and diffract to at least 2.2 A resolution. All the laccase crystals are suitable for X-ray structure determination and contain a full complement of copper ions.
Antorini
Matteo
M
Institute of Biochemistry, Swiss Federal Institute of Technology (ETH), Universitätstrasse 16, CH-8092 Zürich, Switzerland.
Herpoël-Gimbert
Isabelle
I
Choinowski
Thomas
T
Sigoillot
Jean-Claude
JC
Asther
Marcel
M
Winterhalter
Kaspar
K
Piontek
Klaus
K
D001487:Basidiomycota / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D003300:Copper / Q000737:chemistry; D003460:Crystallization; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification; D042845:Laccase; D008031:Lignin / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification*; D014961:X-Ray Diffraction
D007527:Isoenzymes; D003300:Copper; D008031:Lignin; D010088:Oxidoreductases; D042845:Laccase