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Structure paper

TitleStructural basis of fast N-type inactivation in K channels.
Journal, issue, pagesNature, Vol. 645, Issue 8082, Page 1081-1089, Year 2025
Publish dateAug 6, 2025
AuthorsXiao-Feng Tan / Ana I Fernández-Mariño / Yan Li / Tsg-Hui Chang / Kenton J Swartz /
PubMed AbstractAction potentials are generated by opening of voltage-activated sodium (Na) and potassium (K) channels, which can rapidly inactivate to shape the nerve impulse and contribute to synaptic facilitation ...Action potentials are generated by opening of voltage-activated sodium (Na) and potassium (K) channels, which can rapidly inactivate to shape the nerve impulse and contribute to synaptic facilitation and short-term memory. The mechanism of fast inactivation was proposed to involve an intracellular domain that blocks the internal pore in both Na and K channels; however, recent studies in Na and K channels support a mechanism in which the internal pore closes during inactivation. Here we investigate the mechanism of fast inactivation in the Shaker K channel using cryo-electron microscopy, mass spectrometry and electrophysiology. We resolved structures of a fully inactivated state in which the non-polar end of the N terminus plugs the internal pore in an extended conformation. The N-terminal methionine is deleted, leaving an alanine that is acetylated and interacts with a pore-lining isoleucine residue where RNA editing regulates fast inactivation. Opening of the internal activation gate is required for fast inactivation because it enables the plug domain to block the pore and repositions gate residues to interact with and stabilize that domain. We also show that external K destabilizes the inactivated state by altering the conformation of the ion selectivity filter rather than by electrostatic repulsion. These findings establish the mechanism of fast inactivation in K channels, revealing how it is regulated by RNA editing and N-terminal acetylation, and providing a framework for understanding related mechanisms in other voltage-activated channels.
External linksNature / PubMed:40770100 / PubMed Central
MethodsEM (single particle)
Resolution2.67 - 3.2 Å
Structure data

49305

9nec

9ned

EMDB-49305, PDB-9nec:
AcA-EI-shaker with free peptide conformation A
PDB-9ned: AcA-EI-shaker with free peptide conformation B
Method: EM (single particle) / Resolution: 3.2 Å

49308

9neg

EMDB-49308, PDB-9neg:
AcA-EI-shaker Class C
Method: EM (single particle) / Resolution: 3.17 Å

49311

9nei

EMDB-49311, PDB-9nei:
GT-Shaker Class A
Method: EM (single particle) / Resolution: 2.97 Å

49333

9nes

EMDB-49333, PDB-9nes:
C-terminal mVenues tagged Shaker TM domain in C4 symmetry
Method: EM (single particle) / Resolution: 2.67 Å

49336

9neu

EMDB-49336, PDB-9neu:
C-terminal mVenues tagged Shaker T1 domain in C4 symmetry
Method: EM (single particle) / Resolution: 2.98 Å

Chemicals

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

Source
  • drosophila melanogaster (fruit fly)
KeywordsMEMBRANE PROTEIN / voltage-gated potassium channel

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