The author is in the School of Biomedical Sciences, University of Queensland, Brisbane, Queensland 4072, Australia. b.martinac@uq.edu.au
Gating of the mechanosensitive channel MscS involves cooperative action of glycine and alanine residues along the pore-lining transmembrane helix. Opening of the channel is facilitated by an iris-like rotation and tilt of the pore-lining helices. Site-directed mutagenesis indicates that substantial structural plasticity can be tolerated by MscS without impairing its function.
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