2QT6

Crystal Structure Determination of a Blue Laccase from Lentinus Tigrinus

Summary for 2QT6

• Entry DOI: 10.2210/pdb2qt6/pdb
• Descriptor: Laccase, CALCIUM ION, CHLORIDE ION, ... (13 entities in total)
• Functional Keywords: beta barrel, oxidoreductase
• Biological source: Lentinus tigrinus
• Total number of polymer chains: 2
• Total formula weight: 112748.57

Authors

Ferraroni, M.,Briganti, F.,Scozzafava, A. (deposition date: 2007-08-01, release date: 2007-11-20, Last modification date: 2024-12-25)

Primary citation

Ferraroni, M.,Myasoedova, N.M.,Schmatchenko, V.,Leontievsky, A.A.,Golovleva, L.A.,Scozzafava, A.,Briganti, F.
Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases.
Bmc Struct.Biol., 7:60-60, 2007

PubMed Abstract: Laccases belong to multicopper oxidases, a widespread class of enzymes implicated in many oxidative functions in pathogenesis, immunogenesis and morphogenesis of organisms and in the metabolic turnover of complex organic substances. They catalyze the coupling between the four one-electron oxidations of a broad range of substrates with the four-electron reduction of dioxygen to water. These catalytic processes are made possible by the contemporaneous presence of at least four copper ion sites, classified according to their spectroscopic properties: one type 1 (T1) site where the electrons from the reducing substrates are accepted, one type 2 (T2), and a coupled binuclear type 3 pair (T3) which are assembled in a T2/T3 trinuclear cluster where the electrons are transferred to perform the O2 reduction to H2O.

PubMed: 17897461
DOI: 10.1186/1472-6807-7-60

Experimental method

X-RAY DIFFRACTION (1.5 Å)