Molecular modeling of manganese peroxidase from the lignin-degrading fungus Ceriporiopsis subvermispora and structural comparison with other peroxidases

• Mauricio Canales ^[1] ; Sergio Lobos ^[2] ; Rafael Vicuña ^[3]
  1. [1] Universidad de Concepción

     Universidad de Concepción

     Comuna de Concepción, Chile

     
  2. [2] Universidad de Chile

     Universidad de Chile

     Santiago, Chile

     
  3. [3] Pontificia Universidad Católica de Chile

     Pontificia Universidad Católica de Chile

     Santiago, Chile

     

  Mostrar afiliaciones +
• Localización: Electronic Journal of Biotechnology, ISSN-e 0717-3458, Vol. 1, Nº. 2, 1998, págs. 25-96
• Idioma: español
• Enlaces
  • Texto completo
• Resumen

  • Ceriporiopsis subvermispora 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. Based on the crystal structures of MnP and lignin peroxidase (LiP) from P. chrysosporium, and of a peroxidase from Arthromyces ramosus (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.