Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 115, Issue 41, Pages 10333-10338Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1805621115
Keywords
HS-AFM; conformational change; GLIC; Cys-loop; ion channel
Categories
Funding
- Agence Nationale de la Recherche (ANR) Labex Information Flow and Organization at the Membrane (INFORM) [ANR-11-LABX-0054]
- ANR Initiative d'excellence Aix-Marseille (A*MIDEX) program [ANR-11-IDEX-0001-02]
- European Research Council [310080]
- Josie Robertson Investigators Program
- Searle Scholars Program
- European Research Council (ERC) [310080] Funding Source: European Research Council (ERC)
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Gloeobacter violaceus ligand-gated ion channel (GLIC), a proton-gated, cation-selective channel, is a prokaryotic homolog of the pentameric Cys-loop receptor ligand-gated ion channel family. Despite large changes in ion conductance, small conformational changes were detected in X-ray structures of detergent-solubilized GLIC at pH 4 (active/desensitized state) and pH 7 (closed state). Here, we used high-speed atomic force microscopy (HS-AFM) combined with a buffer exchange system to perform structural titration experiments to visualize GLIC gating at the single-molecule level under native conditions. Reference-free 2D classification revealed channels in multiple conformational states during pH gating. We find changes of protein-protein interactions so far elusive and conformational dynamics much larger than previously assumed. Asymmetric pentamers populate early stages of activation, which provides evidence for an intermediate preactivated state.
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