Structural rearrangements underlying K+-channel activation gating.
The intramembrane molecular events underlying activation gating in the Streptomyces K+ channel were investigated by site-directed spin-labeling methods and electron paramagnetic resonance spectroscopy. A comparison of the closed and open conformations of the channel revealed periodic changes in spin-label mobility and intersubunit spin-spin interaction consistent with rigid-body movements of the two transmembrane helices TM1 and TM2. These changes involve translations and counterclockwise rotations of both helices relative to the center of symmetry of the channel. The movement of TM2 increases the diameter of the permeation pathway along the point of convergence of the four subunits, thus opening the pore. Although the extracellular residues flanking the selectivity filter remained immobile during gating, small movements were detected at the C-terminal end of the pore helix, with possible implications to the gating mechanism.
Perozo
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Department of Molecular Physiology and Biological Physics and Center for Structural Biology, University of Virginia Health Sciences Center, Charlottesville, VA 22906-0011, USA. eperozo@virginia.edu
Cortes
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Cuello
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D001426:Bacterial Proteins; D001665:Binding Sites; D002942:Circular Dichroism; D003545:Cysteine / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D015640:Ion Channel Gating; D008958:Models, Molecular; D011188:Potassium / Q000378:metabolism*; D015221:Potassium Channels / Q000737:chemistry* / Q000502:physiology*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012413:Rubidium / Q000378:metabolism; D017384:Sequence Deletion; D013302:Streptomyces / Q000737:chemistry / Q000502:physiology
D001426:Bacterial Proteins; D015221:Potassium Channels; C107790:prokaryotic potassium channel; D003545:Cysteine; D012413:Rubidium; D011188:Potassium