Clostridium difficile Glucosyltransferase Toxin B-essential Amino Acids for Substrate Binding*

@article{Jank2007ClostridiumDG,
  title={Clostridium difficile Glucosyltransferase Toxin B-essential Amino Acids for Substrate Binding*},
  author={T. Jank and T. Giesemann and K. Aktories},
  journal={Journal of Biological Chemistry},
  year={2007},
  volume={282},
  pages={35222 - 35231}
}
Recently the crystal structure of the catalytic domain of Clostridium difficile toxin B was solved ( Reinert, D. J., Jank, T., Aktories, K., and Schulz, G. E. (2005) J. Mol. Biol. 351, 973-981 ). On the basis of this structure, we studied the functional role of several amino acids located in the catalytic center of toxin B. Besides the 286DXD288 motif and Trp102, which were shown to be necessary for Mn2+ and UDP binding, respectively, we identified by alanine scanning Asp270, Arg273, Tyr284… Expand
Crystal structure of Clostridium difficile toxin A
Conformational changes and reaction of clostridial glycosylating toxins.
Identification of an Essential Region for Translocation of Clostridium difficile Toxin B
Structural Determinants of Clostridium difficile Toxin A Glucosyltransferase Activity*
Clostridium perfringens TpeL Glycosylates the Rac and Ras Subfamily Proteins
Bacterial toxin and effector glycosyltransferases.
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The Enterotoxin from Clostridium difficile (ToxA) Monoglucosylates the Rho Proteins(*)
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