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Published November 22, 2002 | Supplemental Material
Journal Article Open

Crystal Structure of Escherichia coli MscS, a Voltage-Modulated and Mechanosensitive Channel

Abstract

The mechanosensitive channel of small conductance (MscS) responds both to stretching of the cell membrane and to membrane depolarization. The crystal structure at 3.9 angstroms resolution demonstrates thatEscherichia coli MscS folds as a membrane-spanning heptamer with a large cytoplasmic region. Each subunit contains three transmembrane helices (TM1, -2, and -3), with the TM3 helices lining the pore, while TM1 and TM2, with membrane-embedded arginines, are likely candidates for the tension and voltage sensors. The transmembrane pore, apparently captured in an open state, connects to a large chamber, formed within the cytoplasmic region, that connects to the cytoplasm through openings that may function as molecular filters. Although MscS is likely to be structurally distinct from other ion channels, similarities in gating mechanisms suggest common structural elements.

Additional Information

© 2002 American Association for the Advancement of Science. Received 30 August 2002; accepted 7 October 2002. Supported by NIH (D.C.R.) and by a National Service Research Award postdoctoral fellowship (R.B.B.). Discussions with R. Spencer, K. Locher, A. Lee, O. Einsle, D. Dougherty, and H. Lester are greatly appreciated. We thank the staffs at the Advanced Light Source, Advanced Photon Source, National Synchrotron Light Source, and the Stanford Synchrotron Radiation Laboratory (SSRL) facilities for their invaluable assistance. These facilities are funded by the Office of Basic Energy Sciences, U.S. Department of Energy, and NIH. The coordinates have been deposited in the Protein Data Bank (1MXM) for release upon publication.

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