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Publication Detail
Role of the C-terminal domain in the structure and function of tetrameric sodium channels.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Bagnéris C, Decaen PG, Hall BA, Naylor CE, Clapham DE, Kay CW, Wallace BA
  • Publication date:
  • Pagination:
    2465, ?
  • Journal:
    Nat Commun
  • Volume:
  • Country:
  • PII:
  • Language:
  • Keywords:
    Alphaproteobacteria, Amino Acid Sequence, Bacterial Proteins, Crystallography, X-Ray, Electron Spin Resonance Spectroscopy, Escherichia coli, Ion Channel Gating, Molecular Dynamics Simulation, Molecular Sequence Data, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins, Static Electricity, Voltage-Gated Sodium Channels
Voltage-gated sodium channels have essential roles in electrical signalling. Prokaryotic sodium channels are tetramers consisting of transmembrane (TM) voltage-sensing and pore domains, and a cytoplasmic carboxy-terminal domain. Previous crystal structures of bacterial sodium channels revealed the nature of their TM domains but not their C-terminal domains (CTDs). Here, using electron paramagnetic resonance (EPR) spectroscopy combined with molecular dynamics, we show that the CTD of the NavMs channel from Magnetococcus marinus includes a flexible region linking the TM domains to a four-helix coiled-coil bundle. A 2.9 Å resolution crystal structure of the NavMs pore indicates the position of the CTD, which is consistent with the EPR-derived structure. Functional analyses demonstrate that the coiled-coil domain couples inactivation with channel opening, and is enabled by negatively charged residues in the linker region. A mechanism for gating is proposed based on the structure, whereby splaying of the bottom of the pore is possible without requiring unravelling of the coiled-coil.
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