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Open channel structure of MscL and the gating mechanism of mechanosensitive channels

Author

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  • Eduardo Perozo

    (University of Virginia)

  • D. Marien Cortes

    (University of Virginia)

  • Pornthep Sompornpisut

    (University of Virginia
    Chulalongkorn University)

  • Anna Kloda

    (University of Western Australia)

  • Boris Martinac

    (University of Western Australia)

Abstract

Mechanosensitive channels act as membrane-embedded mechano-electrical switches, opening a large water-filled pore in response to lipid bilayer deformations. This process is critical to the response of living organisms to direct physical stimulation, such as in touch, hearing and osmoregulation. Here, we have determined the structural rearrangements that underlie these events in the large prokaryotic mechanosensitive channel (MscL) using electron paramagnetic resonance spectroscopy and site-directed spin labelling. MscL was trapped in both the open and in an intermediate closed state by modulating bilayer morphology. Transition to the intermediate state is characterized by small movements in the first transmembrane helix (TM1). Subsequent transitions to the open state are accompanied by massive rearrangements in both TM1 and TM2, as shown by large increases in probe dynamics, solvent accessibility and the elimination of all intersubunit spin–spin interactions. The open state is highly dynamic, supporting a water-filled pore of at least 25 Å, lined mostly by TM1. These structures suggest a plausible molecular mechanism of gating in mechanosensitive channels.

Suggested Citation

  • Eduardo Perozo & D. Marien Cortes & Pornthep Sompornpisut & Anna Kloda & Boris Martinac, 2002. "Open channel structure of MscL and the gating mechanism of mechanosensitive channels," Nature, Nature, vol. 418(6901), pages 942-948, August.
    • Handle: RePEc:nat:nature:v:418:y:2002:i:6901:d:10.1038_nature00992
    DOI: 10.1038/nature00992
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    Cited by:

    1. Tristan Ursell & Kerwyn Casey Huang & Eric Peterson & Rob Phillips, 2007. "Cooperative Gating and Spatial Organization of Membrane Proteins through Elastic Interactions," PLOS Computational Biology, Public Library of Science, vol. 3(5), pages 1-10, May.
    2. Kenjiro Yoshimura & Kazuko Iida & Hidetoshi Iida, 2021. "MCAs in Arabidopsis are Ca2+-permeable mechanosensitive channels inherently sensitive to membrane tension," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    3. Jonathan Mount & Grigory Maksaev & Brock T. Summers & James A. J. Fitzpatrick & Peng Yuan, 2022. "Structural basis for mechanotransduction in a potassium-dependent mechanosensitive ion channel," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    4. Jin Li & William D. Jamieson & Pantelitsa Dimitriou & Wen Xu & Paul Rohde & Boris Martinac & Matthew Baker & Bruce W. Drinkwater & Oliver K. Castell & David A. Barrow, 2022. "Building programmable multicompartment artificial cells incorporating remotely activated protein channels using microfluidics and acoustic levitation," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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