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Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Cu-depleted' isoforms.
Ducros , V; Brzozowski, A M; Wilson, K S; Ostergaard , P; Schneider , P; Svendson , A; Davies, G J.
Acta Crystallogr D Biol Crystallogr ; 57(Pt 2): 333-6, 2001 Feb.
Article in English | MEDLINE | ID: mdl-11173497

ABSTRACT

Laccases (E.C. 1.10.3.2; benzenediol oxygen oxidoreductases) couple the four-electron reduction of dioxygen to water to four one-electron oxidations of a reducing substrate. The three-dimensional structure of the 'blue' multi-copper oxidase laccase from the fungus Coprinus cinereus at 1.68 A reveals the structural basis for isoforms of the type 2 Cu-depleted species.


Subject(s)
Coprinus/enzymology , Oxidoreductases/chemistry , Binding Sites , Copper/metabolism , Crystallization , Crystallography, X-Ray/methods , Isoenzymes/chemistry , Isoenzymes/isolation & purification , Isoenzymes/metabolism , Laccase , Models, Molecular , Oxidoreductases/isolation & purification , Oxidoreductases/metabolism , Protein Conformation , Protein Structure, Secondary
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