Abstract
Potassium channels form one of the most ubiquitous classes of proteins and are found across all forms of life. Permeation of ions through potassium channels is controlled in different ways, most notably at the lower gate and at the selectivity filter. Here, we focus on the MthK channel, an archaeal calcium-gated potassium channel that has seen wide use as a model system. Particularly, binding of Ca2+ ions opens full-length MthK, possibly also triggering the allosteric coupling between the filter and the gate. To understand the gating behavior in more detail, we apply molecular dynamics (MD) simulations, with and without applied voltage, combined with essential dynamics sampling. This is enabled by the recent availability of both closed and open conformations.
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