The S4 segment of the KvAP channel is located at the protein/lipid interface and is highly dynamic, while the S1 segment is surrounded by other parts of the protein at the contact interface.
This study establishes the general principles of voltage-dependent channel structure in a biological membrane by elucidating the positions and dynamics of the S1 and S4 segments of the KvAP channel.
We have analyzed the local structure and dynamics of the prokaryotic voltage-dependent K+ channel (KvAP) at 0 millivolts, using site-directed spin labeling and electron paramagnetic resonance spectroscopy. We show that the S4 segment is located at the protein/lipid interface, with most of its charges protected from the lipid environment. Structurally, S4 is highly dynamic and is separated into two short helices by a flexible linker. Accessibility and dynamics data indicate that the S1 segment is surrounded by other parts of the protein. We propose that S1 is at the contact interface between the voltage-sensing and pore domains. These results establish the general principles of voltage-dependent channel structure in a biological membrane.
Cuello et al. (Thu,) reported a other. The S4 segment of the KvAP channel is located at the protein/lipid interface and is highly dynamic, while the S1 segment is surrounded by other parts of the protein at the contact interface.
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