Abstract
Acidification of the endosome triggers refolding of the diphtheria toxin translocation T domain resulting in its insertion into lipid bilayer and translocation of its N-terminus with the attached catalytic domain of the toxin across the endosomal membrane. Previously we have demonstrated that the initial stage of this conformational transition, namely the formation of membrane-competent form of the T domain, is triggered by histidine protonation in solution. Here we use a combination of molecular dynamics (MD) simulations, thermodynamic integration, continuum electrostatic methodology and several techniques of fluorescence spectroscopy, as well as circular dichroism, to establish the nature of molecular rearrangements, and the sequence of histidine protonation during acidification.
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