Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 23, Issue 1, Pages 31-36Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3138
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Funding
- US National Institutes of Health (NIH) [HL54171]
- US National Science Foundation [PHY1430124]
- NIH [T32 HL007275, T32 HL125241]
- Direct For Mathematical & Physical Scien
- Division Of Physics [1430124] Funding Source: National Science Foundation
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Crystallography has provided invaluable insights regarding ion-channel selectivity and gating, but to advance understanding to a new level, dynamic views of channel structures within membranes are essential. We labeled tetrameric KirBac1.1 potassium channels with single donor and acceptor fluorophores at different sites and then examined structural dynamics within lipid membranes by single-molecule fluorescence resonance energy transfer (FRET). We found that the extracellular region is structurally rigid in both closed and open states, whereas the N-terminal slide helix undergoes marked conformational fluctuations. The cytoplasmic C-terminal domain fluctuates between two major structural states, both of which become less dynamic and move away from the pore axis and away from the membrane in closed channels. Our results reveal mobile and rigid conformations of functionally relevant KirBac1.1 channel motifs, implying similar dynamics for similar motifs in eukaryotic Kir channels and in cation channels in general.
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