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EnglishA multicopper oxidase, the fungal laccase glycoenzyme from the white-rot basidiomycete fungus Trametes (Funalia) trogii, was crystallized and its crystal structure was solved at 1.58 Å using molecular replacement techniques. Model refinement resulted in R-factor and R-free values of 17.4% and 19.0%, respectively. The T. trogii laccase structural model reveals the presence of a ligand bound to the T1 active site which resembles a ptoluate molecule, such bound compound is most probably a fungal metabolite. The p-toluate is bound into the T1 active site of the laccase forming, with one of the carboxylate oxygens, a H-bond with His455, one of the T1 copper ion ligands, whereas the methyl group presents hydrophobic interactions within a pocket composed by Phe331, Phe336, Pro390 and Val162. The coordination geometries, the bond distances and the oxidation states of the T1 and T2/T3 copper active sites are analyzed and discussed in terms of the enzymatic mechanism and catalytic functionality.
Crystal structure of the blue multicopper oxidase from the white-rot fungus Trametes trogii complexed with p-toluate / I. Matera; A. Gullotto; S. Tilli; M. Ferraroni; A. Scozzafava; F. Briganti. - In: INORGANICA CHIMICA ACTA. - ISSN 0020-1693. - STAMPA. - 361(2008), pp. 4129-4137.
| Titolo: | Crystal structure of the blue multicopper oxidase from the white-rot fungus Trametes trogii complexed with p-toluate | |
| Autori di Ateneo: | ||
| Autori: | MATERA, IRENE; GULLOTTO, ANTONELLA; TILLI, SILVIA; FERRARONI, MARTA; SCOZZAFAVA, ANDREA; BRIGANTI, FABRIZIO | |
| Data di pubblicazione: | 2008 | |
| Rivista: | ||
| Volume: | 361 | |
| Pagina iniziale: | 4129 | |
| Pagina finale: | 4137 | |
| Abstract: | A multicopper oxidase, the fungal laccase glycoenzyme from the white-rot basidiomycete fungus Trametes (Funalia) trogii, was crystallized and its crystal structure was solved at 1.58 Å using molecular replacement techniques. Model refinement resulted in R-factor and R-free values of 17.4% and 19.0%, respectively. The T. trogii laccase structural model reveals the presence of a ligand bound to the T1 active site which resembles a ptoluate molecule, such bound compound is most probably a fungal metabolite. The p-toluate is bound into the T1 active site of the laccase forming, with one of the carboxylate oxygens, a H-bond with His455, one of the T1 copper ion ligands, whereas the methyl group presents hydrophobic interactions within a pocket composed by Phe331, Phe336, Pro390 and Val162. The coordination geometries, the bond distances and the oxidation states of the T1 and T2/T3 copper active sites are analyzed and discussed in terms of the enzymatic mechanism and catalytic functionality. | |
| Handle: | http://hdl.handle.net/2158/371096 | |
| Appare nelle tipologie: | 1a - Articolo su rivista |
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