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Structure of native laccase B from Trametes sp. AH28-2.

Authors
  • Ge, Honghua
  • Gao, Yongxiang
  • Hong, Yuzhi
  • Zhang, Min
  • Xiao, Yazhong
  • Teng, Maikun
  • Niu, Liwen
Type
Published Article
Journal
Acta Crystallographica Section F Structural Biology and Crystallization Communications
Publisher
International Union of Crystallography
Publication Date
Mar 01, 2010
Volume
66
Issue
Pt 3
Pages
254–258
Identifiers
DOI: 10.1107/S1744309110000084
PMID: 20208154
Source
Medline
License
Unknown

Abstract

Fungal laccases are oxidoreductases that belong to the multinuclear copper-containing oxidases. They are able to oxidize a wide range of substrates, preferably phenolic compounds, which makes them suitable for employment in the bioremediation of soil and water as well as in other biotechnological applications. Here, the structural analysis of natural laccase B (LacB) from Trametes sp. AH28-2 is presented. This structure provides the opportunity to study the natural post-translational modifications of the enzyme. The overall fold shows a high homology to those of previously analyzed laccases with known three-dimensional structure. However, LacB contains a new structural element, a protruding loop near the substrate-binding site, compared with the previously reported laccase structures. This unique structural feature may be involved in modulation of the substrate recognition of LacB.

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