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*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

13 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)167-173
Number of pages7
JournalBiophysical Chemistry
Volume116
Issue number2
DOIs
Publication statusPublished - 1 Jul 2005

Keywords

  • Modeling
  • Molecular dynamics
  • Oxidoreductase
  • Peroxidase
  • Phanerochaete chrysosporium

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