Structure of native laccase from Trametes hirsuta at 1.8 A resolution.
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.
Polyakov
Konstantin M
KM
V. A. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia. kostya@eimb.ru
Fedorova
Tatyana V
TV
Stepanova
Elena V
EV
Cherkashin
Evgeny A
EA
Kurzeev
Sergei A
SA
Strokopytov
Boris V
BV
Lamzin
Victor S
VS
Koroleva
Olga V
OV
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*
D003300:Copper; D042845:Laccase