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



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



Nature 418(6901): 2-8



The structural dynamic properties of the intermediate and open conformations of the large prokaryotic mechanosensitive channel (MscL) were investigated. Mechanosensitive channels respond to changes in membrane tension by opening a large water-filled pore in response to lipid bilayer deformations. A total of 55 cysteine mutants, targeted to the 2 transmembrane helix segments of MscL, were generated and used to attach a nitroxide spin-label with a methanethiosulphonate moiety. Analysis of individual spectra by electron paramagnetic resonance (EPR) spectroscopy provided information on probe dynamics, solvent accessibility and approximate intersubunit proximities in the conformationally trapped states. This information was compared with a previous site-directed spin labeling/EPR study of MscL in order to produce 3-D models of MscL at various stages of the gating process.

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Accession: 009929702

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