| Registro completo |
| Provedor de dados: |
Electron. J. Biotechnol.
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| País: |
Chile
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| Título: |
Molecular modeling of manganese peroxidase from the lignin-degrading fungus Ceriporiopsis subvermispora and structural comparison with other peroxidases
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| Autores: |
Canales,Mauricio
Lobos,Sergio
Vicuña,Rafael
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| Data: |
1998-08-01
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| Ano: |
1998
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| Resumo: |
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.
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| Tipo: |
Journal article
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34581998000200006
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| Editor: |
Pontificia Universidad Católica de Valparaíso
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| Formato: |
text/html
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| Fonte: |
Electronic Journal of Biotechnology v.1 n.2 1998
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