pH-triggered conformational switching of the diphtheria toxin T-domain: the roles of N-terminal histidines.

@article{Kurnikov2013pHtriggeredCS,
  title={pH-triggered conformational switching of the diphtheria toxin T-domain: the roles of N-terminal histidines.},
  author={Igor Kurnikov and Alexander Kyrychenko and Jose C. Flores-Canales and Mykola V. Rodnin and Nikolay Simakov and Mauricio Vargas-Uribe and Yevgen O. Posokhov and Maria Kurnikova and Alexey S. Ladokhin},
  journal={Journal of molecular biology},
  year={2013},
  volume={425 15},
  pages={2752-64}
}
pH-induced conformational switching is essential for functioning of diphtheria toxin, which undergoes a membrane insertion/translocation transition triggered by endosomal acidification as a key step of cellular entry. In order to establish the sequence of molecular rearrangements and side-chain protonation accompanying the formation of the membrane-competent state of the toxin's translocation (T) domain, we have developed and applied an integrated approach that combines multiple techniques of… CONTINUE READING