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Science 321 (5893): 1179-1183

Copyright © 2008 by the American Association for the Advancement of Science

The Structure of an Open Form of an E. coli Mechanosensitive Channel at 3.45 Å Resolution

Wenjian Wang,1* Susan S. Black,2* Michelle D. Edwards,2* Samantha Miller,2 Emma L. Morrison,2 Wendy Bartlett,2 Changjiang Dong,1 James H. Naismith,1{dagger} Ian R. Booth2{dagger}

Abstract: 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 ~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.

1 Centre for Biomolecular Sciences, The North Haugh, University of St. Andrews, KY16 9ST, Scotland, UK.
2 School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, AB25 2ZD, Scotland, UK.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: naismith{at}st-and.ac.uk (J.H.N.); i.r.booth{at}abdn.ac.uk (I.R.B.)

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
State-stabilizing Interactions in Bacterial Mechanosensitive Channel Gating and Adaptation.
A. Anishkin and S. Sukharev (2009)
J. Biol. Chem. 284, 19153-19157
   Abstract »    Full Text »    PDF »
HIGHLIGHTS FROM THE LITERATURE.
(2008)
Physiology 23, 310-312
   Full Text »    PDF »

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