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

Source: Biophysical chemistry. Vol. 116 (2005): pages 167-173

Author(s)Larrondo, Luis F.; Gonzalez, Angel; Perez-Acle, Tomas; Cullen, Dan; Vicuna, Rafael

Publication Year: 2005  View PDF »

Category: Journal Articles

Abstract: 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.

Keywords: Oxidoreductase, peroxidase, Phanerochaete chrysosporium, modeling, molecular dynamics

File size: 373 kb(s)

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RITS Product ID: 21337
Current FPL Scientist associated with this product
Cullen, Daniel
Research Microbiologist
  

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