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. Author manuscript; available in PMC: 2019 Apr 1.
Published in final edited form as: Biochim Biophys Acta Biomembr. 2017 Dec 16;1860(4):927–942. doi: 10.1016/j.bbamem.2017.12.013

Figure 2.

Figure 2

Potassium channel gating models. (A) Functional and computational experiments suggest that in MthK, the pore-lining helices do not form a tight bundle-crossing when channels are in the closed state; instead these helices appear to mediate a conformational change in the cytosolic domains to gate K+ permeation at the selectivity filter. (B) In KcsA, conformational changes at the bundle-crossing lead to channel opening, and these movements are coupled to closing at the selectivity filter (inactivation).