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

Luis F. Larrondo, Angel Gonzalez, Tomas Perez-Acle, Dan Cullen, Rafael Vicuña

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

13 Citas (Scopus)

Resumen

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.

Idioma originalInglés
Páginas (desde-hasta)167-173
Número de páginas7
PublicaciónBiophysical Chemistry
Volumen116
N.º2
DOI
EstadoPublicada - 1 jul 2005

Áreas temáticas de ASJC Scopus

  • Biofísica
  • Bioquímica
  • Química orgánica

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