A preliminary X-ray diffraction study of the laccase from Coriolus zonatus in the native state
- Russian Academy of Sciences, Shubnikov Institute of Crystallography (Russian Federation)
- Russian Academy of Sciences, Bach Institute of Biochemistry (Russian Federation)
- European Molecular Biology Laboratory (Germany)
- University of St. Andrews, Centre for Biomolecular Sciences (United Kingdom)
The copper-containing enzyme laccase is involved, owing to its oxidase activity, in the biodegradation of lignins-one of the most important bioconversion processes. On the basis of the X-ray diffraction data for the laccase from Coriolus zonatus, the spatial structure of this enzyme is determined with a resolution of 3.2 A. R and R{sub free} are 0.2347 and 0.2976, respectively, and the rms deviations of the bond lengths and the bond angles are 0.009 and 1.547 A, respectively. The three-domain structure of the laccase from Coriolus zonatus is confirmed, where each domain is represented by a protein from the cupredoxin family. The spatial organization of the active center of the protein is established. The mononuclear center contains a copper ion Cu(1) with the atoms of S{sub C}ys453, ND1{sub H}is395, and ND1{sub H}is458 ligands. The trinuclear center is formed by copper ions Cu(2), Cu(3), and Cu(4), surrounded by ligands of eight nitrogen atoms of the histidines of the first and third domains of the protein His66, His109, His454, His111, His400, His452, His64, and His398. The Cu(1) ion is located at distances of 11.84 and 13.22 A from the Cu(2) and Cu(3) ions, respectively. The distance between the Cu(2) and Cu(3) ions is 5.14 A and the Cu(4)-Cu(2) and Cu(4)-Cu(3) distances are 4.75 and 4.41 A, respectively.
- OSTI ID:
- 21091495
- Journal Information:
- Crystallography Reports, Vol. 51, Issue 2; Other Information: DOI: 10.1134/S1063774506020143; Copyright (c) 2006 Nauka/Interperiodica; Article Copyright (c) 2006 Pleiades Publishing, Inc; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7745
- Country of Publication:
- United States
- Language:
- English
Similar Records
Effect of the L499M mutation of the ascomycetous Botrytis aclada laccase on redox potential and catalytic properties
Structure and Biochemestry of Laccases from the Lignin-Degrading Basidiomycete, Ganoderma lucidum