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Sci. Signal., 2 September 2008
Vol. 1, Issue 35, p. ec311
[DOI: 10.1126/scisignal.135ec311]

EDITORS' CHOICE

Structural Biology Channel Opening

Valda J. Vinson

Science, AAAS, Washington, DC 20005, USA

The Escherichia coli mechanosensitive channel, MscS, opens in response to membrane tension to allow ion efflux so that bacteria can survive hypoosmotic shock. Now two papers provide insight into the molecular basis of channel gating (see the Perspective by Gandhi and Rees). Wang et al. determined the crystal structure of the MscS channel in an open conformation, and Vasquez et al. obtained electron paramagnetic resonance measurements on the open conformation in a lipid bilayer. Comparison with a previously determined closed state structure combined with functional data or computational analysis allowed modeling of the movements of the transmembrane helices that cause channel opening.

W. Wang, S. S. Black, M. D. Edwards, S. Miller, E. L. Morrison, W. Bartlett, C. Dong, J. H. Naismith, I. R. Booth, The structure of an open form of an E. coli mechanosensitive channel at 3.45 Å resolution. Science 321, 1179-1183 (2008). [Abstract] [Full Text]

V. Vásquez, M. Sotomayor, J. Cordero-Morales, K. Schulten, E. Perozo, A structural mechanism for MscS gating in lipid bilayers. Science 321, 1210-1214 (2008). [Abstract] [Full Text]

C. S. Gandhi, D. C. Rees, Opening the molecular floodgates. Science 321, 1166-1167 (2008). [Summary] [Full Text]

Citation: V. J. Vinson, Channel Opening. Sci. Signal. 1, ec311 (2008).


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