An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation

Corry, Ben, Hurst, Annette C., Pal, Prithwish, Nomura, Takeshi, Rigby, Paul and Martinac, Boris (2010) An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation. Journal of General Physiology, 136 4: 483-494.


Author Corry, Ben
Hurst, Annette C.
Pal, Prithwish
Nomura, Takeshi
Rigby, Paul
Martinac, Boris
Title An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation
Journal name Journal of General Physiology  (ERA 2012 Listed)    (ERA 2010 Rank B)   Check publisher's open access policy
Publication date 2010-10
Sub-type Article
DOI 10.1085/jgp.200910376
Volume number 136
Issue number 4
ISSN 0022-1295; 1540-7748
Start page 483
End page 494
Total pages 12
Place of publication New York, United States
Publisher Rockefeller University Press
Collection year 2011
Language eng
Abstract Mechanosensitive channels act as molecular transducers of mechanical force exerted on the membrane of living cells by opening in response to membrane bilayer deformations occurring in physiological processes such as touch, hearing, blood pressure regulation, and osmoregulation. Here, we determine the likely structure of the open state of the mechanosensitive channel of large conductance using a combination of patch clamp, fluorescence resonance energy transfer (FRET) spectroscopy, data from previous electron paramagnetic resonance experiments, and molecular and Brownian dynamics simulations. We show that structural rearrangements of the protein can be measured in similar conditions as patch clamp recordings while controlling the state of the pore in its natural lipid environment by modifying the lateral pressure distribution via the lipid bilayer. Transition to the open state is less dramatic than previously proposed, while the N terminus remains anchored at the surface of the membrane where it can either guide the tilt of or directly translate membrane tension to the conformation of the pore-lining helix. Combining FRET data obtained in physiological conditions with simulations is likely to be of great value for studying conformational changes in a range of multimeric membrane proteins. © 2010 Corry et al.
Keyword Mechanosensitive ion channel
Molecular-dynamics simulations
Of-function mutations
Escherichia coli
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article
Collections: Official 2011 Collection
School of Biomedical Sciences Publications
 
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Created: Sun, 19 Dec 2010, 00:10:09 EST