Voltage-dependent gating at the KcsA selectivity filter.
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.
Cordero-Morales
Julio F
JF
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22906, USA.
Cuello
Luis G
LG
Perozo
Eduardo
E
D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D015640:Ion Channel Gating; D008564:Membrane Potentials; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D015221:Potassium Channels / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D048170:Streptomyces lividans / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D015221:Potassium Channels; D011994:Recombinant Proteins; C107790:prokaryotic potassium channel