title: Structure and mechanism in prokaryotic mechanosensitive channels.
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.
authors.affiliation: Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA.
authors.forename: Eduardo
authors.initials: E
authors.lastname: Perozo
authors.forename: Douglas C
authors.initials: DC
authors.lastname: Rees
mesh_terms: D002462:Cell Membrane / Q000235:genetics / Q000502:physiology*; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology; D029968:Escherichia coli Proteins / Q000235:genetics / Q000502:physiology*; D007473:Ion Channels / Q000235:genetics / Q000502:physiology*; D040542:Mechanotransduction, Cellular / Q000235:genetics / Q000502:physiology*
chemical_list: D029968:Escherichia coli Proteins; D007473:Ion Channels; C086596:MscL protein, E coli; C469542:MscS protein, E coli