The oligomeric state of the truncated mechanosensitive channel of large conductance shows no variance in vivo.

ABSTRACT: The mechanosensitive channel of large conductance (MscL) from E. coli serves as an emergency release valve allowing the cell to survive acute osmotic downshock. It is one of the best studied mechanosensitive channels and serves as a paradigm for how a protein can sense and respond to membrane tension. Two MscL crystal structures of the orthologs M. tuberculosis and S. aureus have been solved showing pentameric and tetrameric structures, respectively. Several studies followed to understand whether the discrepancy in their stoichiometry was a species difference or a consequence of the protein manipulation for crystallization. Two independent studies now agree that the full-length S. aureus MscL is actually a pentamer, not tetramer. While detergents appear to play a role in modifying the olig

SUBMITTER: Iscla I 

PROVIDER: S-EPMC3190158 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature