Crystal structure of the blue multicopper oxidase from the white-rot fungus Trametes trogii complexed with p-toluate
作者： Irene Matera , Antonella Gullotto , Silvia Tilli , Marta Ferraroni , Andrea Scozzafava
DOI: 10.1016/J.ICA.2008.03.091
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摘要: Abstract A multicopper oxidase, the fungal laccase glycoenzyme from white-rot basidiomycete fungus Trametes (Funalia) trogii, was crystallized and its crystal structure solved at 1.58 A using molecular replacement techniques. Model refinement resulted in R-factor R-free values of 17.4% 19.0%, respectively. The T. trogii structural model reveals presence a ligand bound to T1 active site which resembles p-toluate molecule, such compound is most probably metabolite. into forming, with one carboxylate oxygens, H-bond His455, copper ion ligands, whereas methyl group presents hydrophobic interactions within pocket composed by Phe331, Phe336, Pro390 Val162. coordination geometries, bond distances oxidation states T2/T3 sites are analyzed discussed terms enzymatic mechanism catalytic functionality.
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