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Electronic Journal of Biotechnology
Universidad Católica de Valparaíso
ISSN: 0717-3458
Vol. 1, No. 2, 1998, pp. 96-102
Bioline Code: ej98013
Full paper language: English
Document type: Research Article
Document available free of charge

Electronic Journal of Biotechnology, Vol. 1, No. 2, 1998, pp. 96-102

 en Molecular modeling of manganese peroxidase from the lignin-degrading fungus Ceriporiopsis subvermispora check for this species in other resources and structural comparison with other peroxidases
Canales, Mauricio; Lobos, Sergio & Vicuña, Rafael

Abstract

Ceriporiopsis subvermispora check for this species in other resources is a white-rot basidiomycete that produces several isoenzymes of manganese peroxidase (MnP•). A cDNA of one of them (MnP13-1) has been isolated and sequenced. The deduced aminoacid sequence shows about 60% similarity with the MnPs from Phanerochaete chrysosporium check for this species in other resources . Based on the crystal structures of MnP and lignin peroxidase (LiP) from P. chrysosporium, and of a peroxidase from Arthromyces ramosus check for this species in other resources (ARP), we have modeled by homology the three dimensional structure of MnP13-1 using standard modeling procedures. Local molecular mechanics optimization performed in the region corresponding to the binding sites of Ca2+ and Mn2+ in MnP13-1 demonstrated that the stereochemistry and the geometry of binding are conserved in both MnPs. A putative aromatic binding site in MnP13-1 is described. We also report structural differences between the two MnPs, arising from the insertion in MnP13-1 of the sequences TGGN between residues S230 and D231 and TDSP at the C-terminal, both of which may have functional significance.

Keywords
Lignin peroxidase, Manganese peroxidase, Molecular modeling, Sequence alignment, Structural comparison

 
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