Chemical Research in Chinese Universities ›› 2017, Vol. 33 ›› Issue (5): 731-735.doi: 10.1007/s40242-017-7142-6

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Insights into the Interactions Between Corrinoid Iron-sulfur Protein and Methyl Transferase from Human Pathogen Clostridium difficile

WEI Yaozhu, TAN Xiangshi   

  1. Shanghai Key Laboratory of Chemical Biology for Protein Research, Department of Chemistry, Fudan University, Shanghai 200433, P. R. China
  • Received:2017-04-13 Revised:2017-07-04 Online:2017-10-01 Published:2017-07-21
  • Contact: TAN Xiangshi,E-mail:xstan@fudan.edu.cn E-mail:xstan@fudan.edu.cn
  • Supported by:

    Supported by the National Natural Science Foundation of China(Nos.31270869, 31670817, 21472027, 91013001);the PhD Program of the Ministry of Education of China(No.20100071110011).

Abstract:

The human pathogen Clostridium difficile infection(CDI) is one of the most important healthcareassociated infections. Methyltransferase(MeTrCd) and corrinoid iron-sulfur protein(CoFeSPCd) are two key proteins in the acetyl-coenzyme A synthesis pathway of Clostridium difficile, which is essential for the survival of the pathogen and is absent in humans. Hence, the interaction between MeTrCd and CoFeSPCd can become innovative targets for the treatment of human CDI. In this study, the interaction between MeTrCd and CoFeSPCd was verified by fluorescence resonance energy transfer measurements. The influence of the interaction on the tertiary structure of MeTrCd and CoFeSPCd was studied by ANS-labeled fluorescence measurements. Molecular docking was also performed tounderstand the mechanism of the protein interactions. These results provide a molecular basis for innovative drug design and development to treat human CDI.

Key words: Corrinoid iron-sulfur protein, Methyl transferase, Clostridium difficile, Protein interaction