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TitleStructure of the Na1.4-β1 Complex from Electric Eel.
Journal, issue, pagesCell, Vol. 170, Issue 3, Page 470-482.e11, Year 2017
Publish dateJul 27, 2017
AuthorsZhen Yan / Qiang Zhou / Lin Wang / Jianping Wu / Yanyu Zhao / Gaoxingyu Huang / Wei Peng / Huaizong Shen / Jianlin Lei / Nieng Yan /
PubMed AbstractVoltage-gated sodium (Na) channels initiate and propagate action potentials. Here, we present the cryo-EM structure of EeNa1.4, the Na channel from electric eel, in complex with the β1 subunit at 4. ...Voltage-gated sodium (Na) channels initiate and propagate action potentials. Here, we present the cryo-EM structure of EeNa1.4, the Na channel from electric eel, in complex with the β1 subunit at 4.0 Å resolution. The immunoglobulin domain of β1 docks onto the extracellular L5 and L6 loops of EeNa1.4 via extensive polar interactions, and the single transmembrane helix interacts with the third voltage-sensing domain (VSD). The VSDs exhibit "up" conformations, while the intracellular gate of the pore domain is kept open by a digitonin-like molecule. Structural comparison with closed NaPaS shows that the outward transfer of gating charges is coupled to the iris-like pore domain dilation through intricate force transmissions involving multiple channel segments. The IFM fast inactivation motif on the III-IV linker is plugged into the corner enclosed by the outer S4-S5 and inner S6 segments in repeats III and IV, suggesting a potential allosteric blocking mechanism for fast inactivation.
External linksCell / PubMed:28735751
MethodsEM (single particle)
Resolution4.0 Å
Structure data

6770

5xsy

EMDB-6770, PDB-5xsy:
Structure of the Nav1.4-beta1 complex from electric eel
Method: EM (single particle) / Resolution: 4.0 Å

Source
  • electrophorus electricus (electric eel)
  • Electric eel (electric eel)
KeywordsMEMBRANE PROTEIN / voltage gated sodium channel

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