Structural determinants of Clostridium difficile toxin A glucosyltransferase activity.

@article{Pruitt2012StructuralDO,
  title={Structural determinants of Clostridium difficile toxin A glucosyltransferase activity.},
  author={Rory N Pruitt and Nicole M. Chumbler and Stacey A. Rutherford and Melissa Ann Farrow and David B Friedman and Ben Spiller and D Borden Lacy},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 11},
  pages={8013-20}
}
The principle virulence factors in Clostridium difficile pathogenesis are TcdA and TcdB, homologous glucosyltransferases capable of inactivating small GTPases within the host cell. We present crystal structures of the TcdA glucosyltransferase domain in the presence and absence of the co-substrate UDP-glucose. Although the enzymatic core is similar to that of TcdB, the proposed GTPase-binding surface differs significantly. We show that TcdA is comparable with TcdB in its modification of Rho… CONTINUE READING