Structural highlights
Publication Abstract from PubMed
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.
Structure of native laccase from Trametes hirsuta at 1.8 A resolution.,Polyakov KM, Fedorova TV, Stepanova EV, Cherkashin EA, Kurzeev SA, Strokopytov BV, Lamzin VS, Koroleva OV Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):611-7. Epub 2009, May 15. PMID:19465775[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Polyakov KM, Fedorova TV, Stepanova EV, Cherkashin EA, Kurzeev SA, Strokopytov BV, Lamzin VS, Koroleva OV. Structure of native laccase from Trametes hirsuta at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):611-7. Epub 2009, May 15. PMID:19465775 doi:10.1107/S0907444909011950