J4 ›› 2013, Vol. 12 ›› Issue (10): 41-43.

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Structure Homology Modeling of Nematode-Trapping Fungus Serine Protease PII

  

  1. 1. College of Agriculture and Biology Science, Dali University, Dali,Yunnan 671003, China;2.Laboratory for Conservation and Utilization of Bio-Resources & Key Laboratory for Microbial Resources of the Ministry of Education, Yunnan University, Kunming 650091, China
  • Received:2013-06-01 Revised:2013-07-03 Online:2013-10-15 Published:2013-10-15

Abstract:

In this article, structural model of Nematode-trapping fungus serine protease PII is constructed and analyzed. The results show that the structural model of PII has the common α/β scaffold characteristics of subtilisin-like serine protease. The catalytic triad residues Asp, His and Ser and the component of oxianion hole residue Asn are completely conserved. The structural model has an overall highly rigid globular fold architecture and do not have disulfide bond. The results of this article will provide a solid basis for further studying the relationship between structure and function of PII.

Key words: serine protease PII, structural model, homology modeling, structure and function relationship

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