Primary structure deduction and molecular modelling from a cDNA of a cellobiohydrolase-like protein from the white-rot fungus Coriolus versicolor.
Molecular cloning and cDNA sequencing analysis were used to elucidate the primary structure of a cellulase-like structure from the white-rot fungus Coriolus versicolor. The cDNA of interest was isolated from a cDNA library obtained from C. versicolor mycelia grown on cellulase inducer medium. A pattern search showed that this cellulase belongs to the glycosyl hydrolases family 6. From the deduced amino acid sequence, models of the binding and catalytic domains were built by homology modelling. The constructed models present a typical cellulose-binding domain at the N-terminal region, a rich Pro, Ser, Thr linker peptide, and a catalytic domain at the C-terminus region.
Novo
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C
INETI/DB/UTPAM, Edifício F, Estrada do Paço do Lumiar 1649-038, Lisbon, Portugal. carlos.novo@mail.ineti.pt
Simões
F
F
Mendonça
D
D
Matos
J
J
Clemente
A
A
D000595:Amino Acid Sequence; D001483:Base Sequence; D002480:Cellulase / Q000737:chemistry* / Q000378:metabolism; D043366:Cellulose 1,4-beta-Cellobiosidase; D018076:DNA, Complementary; D004271:DNA, Fungal; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020072:Polyporales / Q000201:enzymology* / Q000235:genetics; D011487:Protein Conformation; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D004271:DNA, Fungal; D002480:Cellulase; D043366:Cellulose 1,4-beta-Cellobiosidase