Fig. 5 Binding dynamics of the noninactivating channel.

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Fig. 5 Binding dynamics of the noninactivating channel. Binding dynamics of the noninactivating channel. (A) Side view of the KcsA channel and enlarged view of the selectivity filter region with the conductive state (PDB ID: 1K4C) and the collapsed state (1K4D). (B) Height transitions of the E71A and WT channels upon AgTx2 binding. White and black arrowheads indicate the AgTx2-bound and AgTx2-unbound states of the channels, respectively. The noninactivating mutant (E71A) showed markedly high affinity to AgTx2 compared with WT. The binding probabilities of AgTx2 to the E71A mutant obtained by HS-AFM imaging and simulation with only the high-affinity channel are plotted in Fig. 4B. (C and D) Time course of Pbound immediately after or for a persistence of up to 1 or 0.3 s from the dissociation (C) and the binding (D) events. Δt is the time elapsed from the end of tpersist. The height transitions used in this analysis were measured in 10 mM Hepes (pH 7.5) containing 200 mM KCl and 20 nM AgTx2. A. Sumino et al. Sci Adv 2019;5:eaax0495 Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).