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Science 2 July 1999: Vol. 285. no. 5424, pp. 73 - 78 DOI: 10.1126/science.285.5424.73
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Research Articles
Structural Rearrangements Underlying K+-Channel Activation Gating
Eduardo Perozo,
*
D. Marien
,
Cortes,
Luis G. Cuello
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.
Department of Molecular Physiology and Biological Physics and
Center for Structural Biology, University of Virginia Health Sciences
Center, Charlottesville, VA 22906-0011, USA.
*
To whom correspondence should be addressed. E-mail:
eperozo{at}virginia.edu
Read the Full Text
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- A Mutation in the C. elegans EXP-2 Potassium Channel That Alters Feeding Behavior.
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