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Structural plasticity in MS channels

Nature Structural & Molecular Biology volume 12, pages 104–105 (2005)Cite this article

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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Figure 1: Activity and structure of MscS from E. coli.
Figure 2: The pore structure of the MscS channel in the open and closed states.

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Acknowledgements

I would like to thank G. Meyer and P. Rigby for technical assistance.

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  1. School of Biomedical Sciences, University of Queensland, Brisbane, 4072, Queensland, Australia

    Boris Martinac

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  1. Boris Martinac
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Martinac, B. Structural plasticity in MS channels. Nat Struct Mol Biol 12, 104–105 (2005). https://doi.org/10.1038/nsmb0205-104

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