Combined sequence and structure analysis of the fungal laccase family

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Combined sequence and structure analysis of the fungal laccase family

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dc.contributor.author KUMAR, SVS en_US
dc.contributor.author PHALE, PS en_US
dc.contributor.author DURANI, S en_US
dc.contributor.author WANGIKAR, PP en_US
dc.date.accessioned 2011-08-04T11:58:59Z en_US
dc.date.accessioned 2011-12-26T12:54:42Z en_US
dc.date.accessioned 2011-12-27T05:42:54Z
dc.date.available 2011-08-04T11:58:59Z en_US
dc.date.available 2011-12-26T12:54:42Z en_US
dc.date.available 2011-12-27T05:42:54Z
dc.date.issued 2003 en_US
dc.identifier.citation BIOTECHNOLOGY AND BIOENGINEERING, 83(4), 386-394 en_US
dc.identifier.issn 0006-3592 en_US
dc.identifier.uri http://dx.doi.org/10.1002/bit.10681 en_US
dc.identifier.uri http://dspace.library.iitb.ac.in/xmlui/handle/10054/9351 en_US
dc.identifier.uri http://hdl.handle.net/10054/9351
dc.description.abstract Plant and fungal laccases belong to the family of multi-copper oxidases and show much broader substrate specificity than other members of the family. Laccases have consequently been of interest for potential industrial applications. We have analyzed the essential sequence features of fungal laccases based on multiple sequence alignments of more than 100 laccases. This has resulted in identification of a set of four ungapped sequence regions, L1-L4, as the overall signature sequences that can be used to identify the laccases, distinguishing them within the broader class of multi-copper oxidases. The 12 amino acid residues in the enzymes serving as the copper ligands are housed within these four identified conserved regions, of which L2 and L4 conform to the earlier reported copper signature sequences of multi-copper oxidases while L1 and L3 are distinctive to the laccases. The mapping of regions L1-L4 on to the three-dimensional structure of the Coprinus cinerius laccase indicates that many of the non-copper-ligating residues of the conserved regions could be critical in maintaining a specific, more or less C-2 symmetric, protein conformational motif characterizing the active site apparatus of the enzymes. The observed intraprotein homologies between L1 and L3 and between L2 and L4 at both the structure and the sequence levels suggest that the quasi C-2 symmetric active site conformational motif may have arisen from a structural duplication event that neither the sequence homology analysis nor the structure homology analysis alone would have unraveled. Although the sequence and structure homology is not detectable in the rest of the protein, the relative orientation of region L1 with L2 is similar to that of L3 with L4. The structure duplication of first-shell and second-shell residues has become cryptic because the intraprotein sequence homology noticeable for a given laccase becomes significant only after comparing the conservation pattern in several fungal laccases. The identified motifs, L1-L4, can be useful in searching the newly sequenced genomes for putative laccase enzymes. (C) 2003 . en_US
dc.language.iso en en_US
dc.publisher JOHN WILEY & SONS INC en_US
dc.subject white-rot fungus en_US
dc.subject aspergillus-nidulans en_US
dc.subject coprinus-cinereus en_US
dc.subject angstrom resolution en_US
dc.subject molecular-cloning en_US
dc.subject trametes-villosa en_US
dc.subject gene en_US
dc.subject expression en_US
dc.subject purification en_US
dc.subject matrices en_US
dc.subject.other laccases en_US
dc.subject.other multi-copper oxidases en_US
dc.subject.other copper signature sequence en_US
dc.subject.other multiple sequence alignment en_US
dc.subject.other structure alignment en_US
dc.subject.other gene duplication en_US
dc.title Combined sequence and structure analysis of the fungal laccase family en_US
dc.type Article en_US


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