| Literature DB >> 19465775 |
Konstantin M Polyakov1, Tatyana V Fedorova, Elena V Stepanova, Evgeny A Cherkashin, Sergei A Kurzeev, Boris V Strokopytov, Victor S Lamzin, Olga V Koroleva.
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.Entities:
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Year: 2009 PMID: 19465775 DOI: 10.1107/S0907444909011950
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449