The nop gene from Phanerochaete chrysosporium encodes a peroxidase with novel structural features
Larrondo, Luis F. (Pontificia Universidad Católica de Chile)
Gonzalez, Angel (Pontificia Universidad Católica de Chile)
Perez-Acle, T (Pontificia Universidad Católica de Chile)
Cullen, Dan (USDA Forest Products Laboratory)
Vicuña, Rafael (Pontificia Universidad Católica de Chile)

Date:	2005
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.
Note:	Altres ajuts: Millenium Institute for Fundamental and Applied Biology (1030495); U.S. Department of Energy (DE-FG02-87ER13712)
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Language:	Anglès
Document:	Article ; recerca ; Versió sotmesa a revisió
Subject:	Modeling ; Molecular dynamics ; Oxidoreductase ; Peroxidase ; Phanerochaete chrysosporium
Published in:	Biophysical Chemistry, Vol. 116, Núm. 2 (July 2005) , p. 167-173, ISSN 1873-4200

DOI: 10.1016/j.bpc.2005.03.006
PMID: 15950829

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