5XSY

Structure of the Nav1.4-beta1 complex from electric eel

Summary for 5XSY

• Entry DOI: 10.2210/pdb5xsy/pdb
• EMDB information: 6770
• Descriptor: Sodium channel protein, Voltage-gated sodium channel beta subunit 1, beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: voltage gated sodium channel, membrane protein
• Biological source: Electrophorus electricus (Electric eel); More
• Total number of polymer chains: 2
• Total formula weight: 235271.97

Authors

Yan, Z.,Zhou, Q.,Wu, J.P.,Yan, N. (deposition date: 2017-06-15, release date: 2017-08-09, Last modification date: 2025-07-02)

Primary citation

Yan, Z.,Zhou, Q.,Wang, L.,Wu, J.,Zhao, Y.,Huang, G.,Peng, W.,Shen, H.,Lei, J.,Yan, N.
Structure of the Nav1.4-beta 1 Complex from Electric Eel.
Cell, 170:470-482.e11, 2017

PubMed Abstract: 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.

PubMed: 28735751
DOI: 10.1016/j.cell.2017.06.039

Experimental method

ELECTRON MICROSCOPY (4 Å)