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Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy

Nature Structural Biology volume 5, pages 459–469 (1998)Cite this article

Abstract

The transmembrane organization of a potassium channel from Streptomyces lividans has been studied using site directed spin labeling techniques and electron paramagnetic resonance spectroscopy. In the tetrameric channel complex, two α-helices were identified per monomer and assigned to the amino acid sequence. Probe mobility and accessibility data clearly establish that the first helix (TM1) is located in the perimeter of the channel, showing extensive protein–lipid contacts, while the second helix (TM2) is closer to the four-fold symmetric axis of the channel, lining the intracellular vestibule. A large conformational change in the C-terminal end of TM2 was measured when comparing conditions that favor either the open or closed states. The present data suggest that the diameter of the internal vestibule increases with channel opening.

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Authors and Affiliations

  1. Department of Molecular Physiology and Biological Physics and Center for Structural Biology, University of Virginia Health Sciences Center, Charlottesville, Virginia, 22906-0011, USA

    Eduardo Perozo, D. Marien Cortes & Luis G. Cuello

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  1. Eduardo Perozo
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  2. D. Marien Cortes
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  3. Luis G. Cuello
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Correspondence to Eduardo Perozo.

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Perozo, E., Cortes, D. & Cuello, L. Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy. Nat Struct Mol Biol 5, 459–469 (1998). https://doi.org/10.1038/nsb0698-459

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