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

被引：11

作者：

Larrondo, LF

Gonzalez, A

Perez-Acle, T

Cullen, D

Vicuña, R

机构：

[1] Pontificia Univ Catolica Chile, Fac Ciencias Biol, Dept Mol Genet & Microbiol, Santiago, Chile

[2] Inst Milenio Biol Fundamental & Aplicada, Santiago, Chile

[3] Pontificia Univ Catolica Chile, Ctr Genom & Bioinformat, Santiago, Chile

[4] USDA, Forest Prod Lab, Madison, WI 53705 USA

来源：

BIOPHYSICAL CHEMISTRY | 2005年 / 116卷 / 02期

关键词：

oxidoreductase; peroxidase; Phanerochaete chrysosporium; modeling; molecular dynamics;

D O I：

10.1016/j.bpc.2005.03.006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (c) 2005 Elsevier B.V. All rights reserved.

引用

页码：167 / 173

页数：7

共 41 条

[11]

Feng DF, 1996, METHOD ENZYMOL, V266, P368

[12] Impact of the physical and chemical environment on the molecular structure of Coprinus cinereus peroxidase [J].