The diphtheria toxin channel-forming T-domain translocates its own NH2-terminal region and the catalytic domain across planar phospholipid bilayers
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2016, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :Additional similarities between BoNT and SecY are their high content of α-helices and the fact that the SecY channel may open laterally to the lipid bilayer to release membrane spanning segment of a nascent protein. Also, the diphtheria toxin translocating domain is mainly α-helical and there is evidence that a single molecule is involved in the process with few transmembrane helices forming an ion channel [70,71]. At variance, it was recently reported that a BoNT/B trimer forms the protein conducting transmembrane channel in PC12 cells [35].
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