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Elucidation of the crystal structure of Coriolopsis caperata laccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions.
- Source :
-
Acta Crystallographica: Section D (Wiley-Blackwell) . Apr2015, Vol. 71 Issue 4, p854-861. 8p. - Publication Year :
- 2015
-
Abstract
- Laccases are members of a large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of dioxygen to water. A new laccase was isolated from the basidiomycete Coriolopsis caperata strain 0677 and its amino-acid sequence was determined. According to its physicochemical properties and spectroscopic features, the laccase from C. caperata is a high redox-potential blue laccase. Attempts to crystallize the native enzyme were unsuccessful. The copper type 2-depleted (T2D) laccase was prepared and crystallized. The structure of T2D laccase from C. caperata was solved at 1.6 Å resolution, and attempts to reconstruct the T2 copper centre were performed using Cu+ and Cu2+ ions. The structure of T2D+Cu+ laccase was solved at 1.89 Å resolution. It was shown that the T2D+Cu+ laccase structure contained four copper ions in the active site. Reconstruction could not be achieved when the T2D laccase crystals were treated with CuSO4. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09074449
- Volume :
- 71
- Issue :
- 4
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section D (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 101965719
- Full Text :
- https://doi.org/10.1107/S1399004715001595