| Description | Mechanosensitive (MS) channels provide protection against hypo-osmotic shock, responding both to stretching of the cell membrane and to membrane depolarisation. They are present in the membranes of organisms from the three domains of life: bacteria, archaea, and eukarya [ ]. There are two families of MS channels: large-conductance MS channels (MscL) and small-conductance MS channels (MscS or YGGB). The pressure threshold for MscS opening is 50% that of MscL []. The MscS family is much larger and more variable in size and sequence than the MscL family. Much of the diversity in MscS proteins occurs in the size of the transmembrane regions, which ranges from three to eleven transmembrane helices, although the three C-terminal helices are conserved.MscS folds as a homo-heptamer with a cylindrical shape, and can be divided into transmembrane and extramembrane regions: an N-terminal periplasmic region, a transmembrane region, and a C-terminal cytoplasmic region (middle and C-terminal domains). The transmembrane region forms a channel through the membrane that opens into a chamber enclosed by the extramembrane portion, the latter connecting to the cytoplasm through distinct portals [ , ]. This entry represents the middle domain superfamily of small conductance mechanosensitive channels (MscS), consisting of five β-strands (referred to as β-domain) that pack together with those of other subunits to form a barrel-like sheet extending around the entire protein. In the fission yeast Schizosaccharomyces pombe the mechanosensitive ion channel proteins are known as msy1 and msy2 [ , ]. | Name | Mechanosensitive ion channel MscS, beta-domain superfamily |
| Short Name | MscS_beta-dom_sf | Type | Homologous_superfamily |
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