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Structural titration of receptor ion channel GLIC gating by HS-AFM.


ABSTRACT: 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.

SUBMITTER: Ruan Y 

PROVIDER: S-EPMC6187180 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Structural titration of receptor ion channel GLIC gating by HS-AFM.

Ruan Yi Y   Kao Kevin K   Lefebvre Solène S   Marchesi Arin A   Corringer Pierre-Jean PJ   Hite Richard K RK   Scheuring Simon S  

Proceedings of the National Academy of Sciences of the United States of America 20180904 41


<i>Gloeobacter violaceus</i> 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 perfor  ...[more]

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