The E106/D115 residue pair, equivalent to E71/D80 in KcsA, is not involved in maintenance of K selectivity.(A) Potassium channel SF signature sequence alignments (green) with E106 and D115 equivalent positions in yellow and red, respectively. (B) Crystal structure of KirBac1.1 SF and the hydrogen bond behind SF (E106 in yellow and D115 in red), equivalent to E71–D80 in KcsA. (C) Relative flux calculated as in Fig. 2, for mutants, as indicated. KirBac1.1 hydrogen bond mutants are functional in 150 mM KCl (left) and maintain K selectivity in 150 mM NaCl (right). All data are represented as mean ± SEM of at least n = 3 experiments.
Figure 4.

The E106/D115 residue pair, equivalent to E71/D80 in KcsA, is not involved in maintenance of K selectivity. (A) Potassium channel SF signature sequence alignments (green) with E106 and D115 equivalent positions in yellow and red, respectively. (B) Crystal structure of KirBac1.1 SF and the hydrogen bond behind SF (E106 in yellow and D115 in red), equivalent to E71–D80 in KcsA. (C) Relative flux calculated as in Fig. 2, for mutants, as indicated. KirBac1.1 hydrogen bond mutants are functional in 150 mM KCl (left) and maintain K selectivity in 150 mM NaCl (right). All data are represented as mean ± SEM of at least n = 3 experiments.

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