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Structure and hydration of membranes embedded with voltage-sensing domains

Author

Listed:
  • Dmitriy Krepkiy

    (Molecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA)

  • Mihaela Mihailescu

    (and Center for Biomembrane Systems
    NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland 20899, USA)

  • J. Alfredo Freites

    (and Center for Biomembrane Systems
    Department of Chemistry and Institute for Surface and Interface Science,)

  • Eric V. Schow

    (University of California, Irvine, California 92697, USA)

  • David L. Worcester

    (and Center for Biomembrane Systems
    NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland 20899, USA
    University of Missouri, Columbia, Missouri 65211, USA)

  • Klaus Gawrisch

    (Laboratory of Membrane Biochemistry and Biophysics, National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Bethesda, Maryland 20892, USA)

  • Douglas J. Tobias

    (Department of Chemistry and Institute for Surface and Interface Science,)

  • Stephen H. White

    (and Center for Biomembrane Systems
    NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland 20899, USA)

  • Kenton J. Swartz

    (Molecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA)

Abstract

Despite the growing number of atomic-resolution membrane protein structures, direct structural information about proteins in their native membrane environment is scarce. This problem is particularly relevant in the case of the highly charged S1–S4 voltage-sensing domains responsible for nerve impulses, where interactions with the lipid bilayer are critical for the function of voltage-activated ion channels. Here we use neutron diffraction, solid-state nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics simulations to investigate the structure and hydration of bilayer membranes containing S1–S4 voltage-sensing domains. Our results show that voltage sensors adopt transmembrane orientations and cause a modest reshaping of the surrounding lipid bilayer, and that water molecules intimately interact with the protein within the membrane. These structural findings indicate that voltage sensors have evolved to interact with the lipid membrane while keeping energetic and structural perturbations to a minimum, and that water penetrates the membrane, to hydrate charged residues and shape the transmembrane electric field.

Suggested Citation

  • Dmitriy Krepkiy & Mihaela Mihailescu & J. Alfredo Freites & Eric V. Schow & David L. Worcester & Klaus Gawrisch & Douglas J. Tobias & Stephen H. White & Kenton J. Swartz, 2009. "Structure and hydration of membranes embedded with voltage-sensing domains," Nature, Nature, vol. 462(7272), pages 473-479, November.
    • Handle: RePEc:nat:nature:v:462:y:2009:i:7272:d:10.1038_nature08542
    DOI: 10.1038/nature08542
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