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* Istituto di Chimica del Riconoscimento Molecolare, CNR, 20131 Milan, Italy; and Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Department of Biophysical Chemistry, University of Groningen, 9747 AG Groningen, The Netherlands
Correspondence: Address reprint requests to Giorgio Colombo, Istituto di Chimica del Riconoscimento Molecolare, CNR, via Mario Bianco 9, 20131 Milan, Italy. Tel.: +39-02-28500031; Fax: +39-02-28500036; E-mail: colombo{at}icrm.cnr.it or Alan E. Mark, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Department of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands. Tel.: +31-50-3634457; Fax: +31-50-3634800; E-mail: mark{at}chem.rug.nl.
The initial stages of the gating of the mechanoselective channel of large conductance from Mycobacterium tuberculosis have been studied in atomic detail using molecular dynamics simulation techniques. A truncated form of the protein complex embedded in a palmitoyloleoylphosphatidylcholine lipid bilayer and surrounded by explicit water was simulated under different pressure conditions to mimic the effects of tension and compression within the membrane on the protein. As a direct result of lateral tension being applied to the membrane, an increase in the tilt of a subset of the transmembrane helices was observed. This in turn led to the enlargement of the pore and the disruption of the hydrophobic gate consisting of residues Ile-14 and Val-21. The simulations suggest that opening occurs in a sequential staged process. Such a mechanism could explain the partial opening or staged conductance observed in patch-clamp experiments using related large conductance mechanosensitive channel complexes.
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