X-ray structural studies of the fungal laccase from Cerrena maxima.

Laccases are members of the blue multi-copper oxidase family. These enzymes oxidize substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and following the transfer of four electrons is reduced to two molecules of water. The X-ray structure of a laccase from Cerrena maxima has been elucidated at 1.9 Å resolution using synchrotron data and the molecular replacement technique. The final refinement coefficients are R _cryst = 16.8% and R _free = 23.0%, with root mean square deviations on bond lengths and bond angles of 0.015 Å and 1.51°, respectively. The type 1 copper centre has an isoleucine residue at the axial position and the “resting” state of the trinuclear centre comprises a single oxygen (OH) moiety asymmetrically disposed between the two type 3 copper ions and a water molecule attached to the type 2 ion. Several carbohydrate binding sites have been identified and the glycan chains appear to promote the formation of well-ordered crystals. Two tyrosine residues near the protein surface have been found in a nitrated state. [ABSTRACT FROM AUTHOR]