Document Detail


Structure of native laccase B from Trametes sp. AH28-2.
MedLine Citation:
PMID:  20208154     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Honghua Ge; Yongxiang Gao; Yuzhi Hong; Min Zhang; Yazhong Xiao; Maikun Teng; Liwen Niu
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-02-23
Journal Detail:
Title:  Acta crystallographica. Section F, Structural biology and crystallization communications     Volume:  66     ISSN:  1744-3091     ISO Abbreviation:  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.     Publication Date:  2010 Mar 
Date Detail:
Created Date:  2010-03-08     Completed Date:  2010-04-05     Revised Date:  2013-03-21    
Medline Journal Info:
Nlm Unique ID:  101226117     Medline TA:  Acta Crystallogr Sect F Struct Biol Cryst Commun     Country:  England    
Other Details:
Languages:  eng     Pagination:  254-8     Citation Subset:  IM    
Affiliation:
Modern Experiment Technology Center and School of Life Sciences, Anhui University, Hefei 230039, People's Republic of China.
Data Bank Information
Bank Name/Acc. No.:
PDB/3KW7
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Binding Sites
Conserved Sequence
Crystallography, X-Ray
Laccase / chemistry*,  metabolism
Molecular Sequence Data
Protein Stability
Sequence Alignment
Structural Homology, Protein
Substrate Specificity
Trametes / enzymology*
Chemical
Reg. No./Substance:
EC 1.10.3.2/Laccase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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