The structure of an open form of an E. coli mechanosensitive channel at 3.45 Å resolution

Wenjian Wang, Susan Shirley Black, Michelle D. Edwards, Samantha Miller, Emma Louise Morrison, Wendy Bartlett, Changjiang Dong, James H. Naismith, Ian R. Booth

Research output: Contribution to journalArticle

164 Citations (Scopus)


How ion channels are gated to regulate ion flux in and out of cells is the subject of intense interest. The Escherichia coli mechanosensitive channel, MscS, opens to allow rapid ion efflux, relieving the turgor pressure that would otherwise destroy the cell. We present a 3.45 angstrom-resolution structure for the MscS channel in an open conformation. This structure has a pore diameter of similar to 13 angstroms created by substantial rotational rearrangement of the three transmembrane helices. The structure suggests a molecular mechanism that underlies MscS gating and its decay of conductivity during prolonged activation. Support for this mechanism is provided by single-channel analysis of mutants with altered gating characteristics.

Original languageEnglish
Pages (from-to)1179-1183
Number of pages5
Issue number5893
Publication statusPublished - 29 Aug 2008


  • gated potassium channel
  • acetylcholine-receptor
  • crystal-structure
  • ion-channel
  • K+ channel
  • protein stability
  • MSCS
  • pore
  • mechanism
  • cooperativity


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