The Structure of an Open Form of anE. coliMechanosensitive Channel at 3.45 Å Resolution
- 29 August 2008
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 321 (5893) , 1179-1183
- https://doi.org/10.1126/science.1159262
Abstract
How ion channels are gated to regulate ion flux in and out of cells is the subject of intense interest. TheEscherichia colimechanosensitive 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 ∼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.Keywords
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