3KW7

Crystal structure of LacB from Trametes sp. AH28-2

Summary for 3KW7

• Entry DOI: 10.2210/pdb3kw7/pdb
• Descriptor: Laccase B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (5 entities in total)
• Functional Keywords: laccase, metal-binding, oxidoreductase
• Biological source: Trametes
• Total number of polymer chains: 2
• Total formula weight: 110885.37

Authors

Ge, H.H.,Teng, M.K.,Niu, L.W. (deposition date: 2009-12-01, release date: 2010-03-09, Last modification date: 2024-10-09)

Primary citation

Ge, H.H.,Gao, Y.X.,Hong, Y.Z.,Zhang, M.,Xiao, Y.Z.,Teng, M.K.,Niu, L.W.
Structure of native laccase B from Trametes sp. AH28-2
Acta Crystallogr.,Sect.F, 66:254-258, 2010

PubMed 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.

PubMed: 20208154
DOI: 10.1107/S1744309110000084

Experimental method

X-RAY DIFFRACTION (3.44 Å)