2xyb | pdb_00002xyb
From Proteopedia
CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS
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Structural highlights
Publication Abstract from PubMedLaccase 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. Purification, crystallisation and X-ray diffraction study of fully functional laccases from two ligninolytic fungi.,Antorini M, Herpoel-Gimbert I, Choinowski T, Sigoillot JC, Asther M, Winterhalter K, Piontek K Biochim Biophys Acta. 2002 Jan 31;1594(1):109-14. PMID:11825613[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences | ||||||||||||||||||||
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