The crystal structure of the prokaryotic KirBac1.1 channel in the closed state was refined to 3.65 angstroms, identifying the main activation gate and structural elements involved in gating.
The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main activation gate and structural elements involved in gating. On the basis of structural evidence presented here, we suggest that gating involves coupling between the intracellular and membrane domains. This further suggests that initiation of gating by membrane or intracellular signals represents different entry points to a common mechanistic pathway.
Kuo et al. (Tue,) reported a other. The crystal structure of the prokaryotic KirBac1.1 channel in the closed state was refined to 3.65 angstroms, identifying the main activation gate and structural elements involved in gating.