title: Structure of native laccase from Trametes hirsuta at 1.8 A resolution.
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.
authors.affiliation: V. A. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia. kostya@eimb.ru
authors.forename: Konstantin M
authors.initials: KM
authors.lastname: Polyakov
authors.forename: Tatyana V
authors.initials: TV
authors.lastname: Fedorova
authors.forename: Elena V
authors.initials: EV
authors.lastname: Stepanova
authors.forename: Evgeny A
authors.initials: EA
authors.lastname: Cherkashin
authors.forename: Sergei A
authors.initials: SA
authors.lastname: Kurzeev
authors.forename: Boris V
authors.initials: BV
authors.lastname: Strokopytov
authors.forename: Victor S
authors.initials: VS
authors.lastname: Lamzin
authors.forename: Olga V
authors.initials: OV
authors.lastname: Koroleva
mesh_terms: D020134:Catalytic Domain; D003300:Copper / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D042845:Laccase / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D055454:Trametes / Q000201:enzymology*
chemical_list: D003300:Copper; D042845:Laccase