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. Author manuscript; available in PMC: 2022 Feb 2.
Published in final edited form as: Methods Enzymol. 2021 Feb 2;649:341–370. doi: 10.1016/bs.mie.2020.12.016

Fig. 1.

Fig. 1

(A) Crystallographic structure of the diphtheria toxin translocation domain [Bennett & Eisenberg, 1994; Weiss et al., 1995] consists of several structural elements that undergo conformational changes in response to protonation and membrane interactions. (B) pH-triggered membrane insertion pathway of the diphtheria toxin T-domain [Kurnikov et al., 2013; Kyrychenko, Posokhov, Rodnin, & Ladokhin, 2009], responsible for the cellular entry of the toxin.