Two domain laccase (small laccase) from Streptomyces coelicolor

Years: 2006 - now

PDB code: 3CG8

Laccases (EC 1.10.3.2) are multicopper oxidases catalyzing the reduction of molecular oxygen to water accompanied by oxidation of a substrate, with broad substrate specificity (polyphenols, methoxy-substituted phenols, aromatic diamines). Common laccases consists of three domains. The laccase from Streptomyces coelicolor is the first two-domain laccase structure of which was solved. During 2009, structures of two other two-domain oxidoreductases of subtype C were published. The laccase from Streptomyces coelicolor stays the only solved structure of subtype B.

Multicopper blue proteins form an interesting protein family with variability of positions of copper ions in proteins and variability of protein oligomerization states. An evolutionary theory of multicopper blue proteins was proposed by Nakamura and Go (Cell. Mol. Life. Sci., 62 (18), 2050-2066), with evolution from monomeric proteins over two-domain trimeric proteins of three types (A, B and C) towards three-domain laccases and ascorbate oxidases, two-domain nitrite reductases and six-domain ceruloplasmin.

The structure of laccase from Streptomyces coelicolor confirms basic expectations of Nakamura and Go concerning protein arrangement and brings detailed structural information.

Fig. 1. Laccase from Streptomyces coelicolor. This is an animated figure. Open it in a new window to see the animation.

Publications:

• Skalova, T; Dohnalek, J; Ostergaard, LH; Ostergaard, PR; Kolenko, P; Duskova, J; Stepankova, A; Hasek, J. The structure of the small laccase from Streptomyces coelicolor reveals a link between laccases and nitrite reductases. JOURNAL OF MOLECULAR BIOLOGY, 2009, 385, 1165-1178.

• Skalova, T; Dohnalek, J; Oestergaard, L.H.; Oestergaard, P.R.; Kolenko, P.; Duskova, J.; Hasek, J. Crystallization and preliminary X-ray diffraction analysis of the small laccase from Streptomyces coelicolor. ACTA CRYSTALLOGRAPHICA SECTION F-Structural biology and crystallization communications, 2007, 63, 1077-1079.