Structure and hydration of membranes embedded with voltage-sensing domains

Dmitriy Krepkiy, Mihaela Mihailescu, J. Alfredo Freites, Eric V. Schow, David L. Worcester, Klaus Gawrisch, Douglas J. Tobias, Stephen H. White () and Kenton J. Swartz ()
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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
J. Alfredo Freites: and Center for Biomembrane Systems
Eric V. Schow: University of California, Irvine, California 92697, USA
David L. Worcester: and Center for Biomembrane Systems
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
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

Nature, 2009, vol. 462, issue 7272, 473-479

Abstract: 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.

Date: 2009
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DOI: 10.1038/nature08542

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