Open and Closed Structures of a Barium-Blocked Potassium Channel

钡阻塞钾通道的开放和关闭结构

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Abstract

Barium (Ba(2+)) is a classic permeant blocker of potassium (K(+)) channels. The "external lock-in effect" in barium block experiments, whereby the binding of external K(+) impedes the forward translocation of the blocker, provides a powerful avenue to investigate the selectivity of the binding sites along the pore of potassium channels. Barium block experiments show that the external lock-in site is highly selective for K(+) over Na(+). Wild-type KcsA was crystallized in low K(+) conditions, and the crystals were soaked in solutions containing various concentrations of barium. Structural analysis reveals open and closed gate conformations of the KcsA channel. Anomalous diffraction experiments show that Ba(2+) primarily binds to the innermost site S4 of the selectivity filter of the open-gate conformation and also the site S2, but no binding is detected with the closed-gate conformation. Alchemical free-energy perturbation calculations indicate that the presence of a Ba(2+) ion in the selectivity filter boosts the specificity of K(+) binding relative to Na(+) in the external sites S0-S2.

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