A Caltech Library Service

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

Bass, Randal B. and Strop, Pavel and Barclay, Margaret and Rees, Douglas C. (2002) Crystal Structure of Escherichia coli MscS, a Voltage-Modulated and Mechanosensitive Channel. Science, 298 (5598). pp. 1582-1587. ISSN 0036-8075. doi:10.1126/science.1077945.

PDF - Supplemental Material
See Usage Policy.


Use this Persistent URL to link to this item:


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.

Item Type:Article
Related URLs:
URLURL TypeDescription Online Material
Rees, Douglas C.0000-0003-4073-1185
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.
Funding AgencyGrant Number
National Service Research AwardUNSPECIFIED
Department of Energy (DOE)UNSPECIFIED
Issue or Number:5598
Record Number:CaltechAUTHORS:20141112-142214604
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:51677
Deposited By: Tony Diaz
Deposited On:13 Nov 2014 00:39
Last Modified:13 Apr 2022 17:15

Repository Staff Only: item control page