Characterization of the resting MscS: modeling and analysis of the closed bacterial mechanosensitive channel of small conductance.

ABSTRACT: Channels from the MscS family are adaptive tension-activated osmolyte release valves that regulate turgor in prokaryotes and volume in plant chloroplasts. The crystal structure of Escherichia coli MscS has provided a starting point for detailed descriptions of its mechanism. However, solved in the absence of the lipid bilayer, this structure may deviate from a native conformation. In this study, we utilized molecular dynamics simulations and a new iterative extrapolated-motion protocol to pack the splayed peripheral TM1 and TM2 transmembrane helices along the central TM3 shaft. This modification restored the tension transmission route between the membrane and the channel gate. We also modeled the structure of the 26-amino acid N-terminal segments that were unresolved in the crystals. The r

SUBMITTER: Anishkin A 

PROVIDER: S-EPMC2212706 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature