title: Brownian dynamics investigation into the conductance state of the MscS channel crystal structure.
abstract: We suggest that the crystal structure of the mechanosensitive channel of small conductance is in a minimally conductive state rather than being fully activated. Performing Brownian dynamics simulations on the crystal structure show that no ions pass through it. When simulations are conducted on just the transmembrane domain (excluding the cytoplasmic residues 128 to 280) ions are seen to pass through the channel, but the conductance of approximately 30 pS is well below experimentally measured values. The mutation L109S that replaces a pore lining hydrophobic residue with a polar one is found to have little effect on the conductance of the channel. Widening the hydrophobic region of the pore by 2.5 Angstrom however, increases the channel conductance to over 200 pS suggesting that only a minimal conformational change is required to gate the pore.
authors.affiliation: Department of Theoretical Physics, Research School of Physical Sciences, The Australian National University, Canberra, A.C.T. 0200, Australia.
authors.forename: Taira
authors.initials: T
authors.lastname: Vora
authors.forename: Ben
authors.initials: B
authors.lastname: Corry
authors.forename: Shin-Ho
authors.initials: SH
authors.lastname: Chung
mesh_terms: D003460:Crystallization; D029968:Escherichia coli Proteins / Q000737:chemistry*; D007473:Ion Channels / Q000737:chemistry*; D015394:Molecular Structure
chemical_list: D029968:Escherichia coli Proteins; D007473:Ion Channels; C469542:MscS protein, E coli