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Acta Crystallogr D Biol Crystallogr ; 65(Pt 6): 611-7, 2009 Jun.
Article in English | MEDLINE | ID: mdl-19465775

ABSTRACT

This paper describes the structural analysis of the native form of laccase from Trametes hirsuta at 1.8 A resolution. This structure provides a basis for the elucidation of the mechanism of catalytic action of these ubiquitous proteins. The 1.8 A resolution native structure provided a good level of structural detail compared with many previously reported laccase structures. A brief comparison with the active sites of other laccases is given.


Subject(s)
Crystallography, X-Ray , Laccase/chemistry , Trametes/enzymology , Catalytic Domain , Copper/metabolism , Crystallization , Laccase/metabolism , Protein Conformation , Structure-Activity Relationship
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