Voltage-dependent gating at the KcsA selectivity filter

Nat Struct Mol Biol. 2006 Apr;13(4):319-22. doi: 10.1038/nsmb1070. Epub 2006 Mar 12.


The prokaryotic K(+) channel KcsA, although lacking a 'standard' voltage-sensing domain, shows voltage-dependent gating that leads to an increase in steady-state open probability of almost two orders of magnitude between +150 and -150 mV. Here we show that voltage-dependent gating in KcsA is associated with the movement of approximately 0.7 equivalent electronic charges. This charge movement produces an increase in the rate of entry into a long-lived inactivated state and seems to be independent of the proton-activation mechanism. Charge neutralization at position 71 renders the channel essentially voltage-independent by preventing entry into the inactivated state. A mechanism for voltage-dependent gating at the selectivity filter is proposed that is based on the reorientation of the carboxylic moiety of Glu71 and its influence in the conformational dynamics of the selectivity filter.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Substitution
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Hydrogen-Ion Concentration
  • Ion Channel Gating
  • Membrane Potentials
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Potassium Channels / chemistry
  • Potassium Channels / genetics
  • Potassium Channels / metabolism*
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Streptomyces lividans / genetics
  • Streptomyces lividans / metabolism


  • Bacterial Proteins
  • Potassium Channels
  • Recombinant Proteins
  • prokaryotic potassium channel