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Structure and mechanism in prokaryotic mechanosensitive channels

by: Eduardo Perozo, Douglas C. Rees
Current Opinion in Structural Biology, Vol. 13, No. 4. (August 2003), pp. 432-442, doi:10.1016/s0959-440x(03)00106-4  Key: citeulike:11286701

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Abstract

Mechanosensitive channels function as electromechanical switches with the capability to sense the physical state of lipid bilayers. The X-ray crystal structures of MscL and MscS offer a unique opportunity to identify the types of protein motions associated with the opening and closing of these structurally unrelated channels, while providing the framework to address a mechanism of tension sensing that is defined by channel–lipid interactions. Recent functional, structural and dynamic data offer fresh insights into the molecular basis of gating for these membrane proteins.


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