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Biophys Chem. 2005 Jul 1;116(2):167-73.

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

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Departamento de Genética Molecular y Microbiología, Facultad de Ciencias Biológicas, Pontificia, Universidad Católica de Chile, Santiago, Chile and Instituto Milenio de Biología Fundamental y Aplicada, Alameda 340, Santiago, Chile.


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.

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