The nop gene from Phanerochaete chrysosporium encodes a peroxidase with novel structural features

Inspection of the genome of the ligninolytic basidiomycete Phanerochaete chrysosporium revealed an unusual peroxidase_like sequence. The corresponding full length cDNA was sequenced and an archetypal secretion signal predicted. The deduced mature protein (NoP, novel peroxidase) contains 295 aa resid...

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Bibliographic Details
Published in:Biophysical chemistry 2005-07, Vol.116 (2), p.167-173
Main Authors: Larrondo, LuisF, Gonzalez, Angel, Perez_Acle, Tomas, Cullen, Dan, Vicuña, Rafael
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Crystallography
Genes, Fungal
Modeling
Models, Molecular
Molecular dynamics
Oxidoreductase
Peroxidase
Peroxidases - chemistry
Peroxidases - genetics
Phanerochaete - enzymology
Phanerochaete - genetics
Phanerochaete chrysosporium
Protein Conformation
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Summary:Inspection of the genome of the ligninolytic basidiomycete Phanerochaete chrysosporium revealed an unusual peroxidase_like sequence. The corresponding full length cDNA was sequenced and an archetypal secretion signal predicted. The deduced mature protein (NoP, novel peroxidase) contains 295 aa residues and is therefore considerably shorter than other Class II (fungal) peroxidases, such as lignin peroxidases and manganese peroxidases. Comparative modeling of NoP was conducted using the crystal structures of Coprinus cinereus and Arthromyces ramosus peroxidases as templates. The model was validated by molecular dynamics and showed several novel structural features. In particular, NoP has only three disulfide bridges and tryptophan replaces the distal phenylalanine within the heme pocket.
ISSN:0301-4622
1873-4200
DOI:10.1016/j.bpc.2005.03.006