'Feeling the pressure': structural insights into a gated mechanosensitive channel.
The structure determination of the large-conductance mechanosensitive channel (MscL) from Mycobacterium tuberculosis has revealed the architecture of the first full-length, gated pentameric ion channel. This structure provides insights into the elements participating in the conductance and gating mechanisms of these channels.
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Howard Hughes Medical Institute, Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA.
Chang
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D000595:Amino Acid Sequence; D001419:Bacteria / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins; D015640:Ion Channel Gating / Q000502:physiology*; D007473:Ion Channels / Q000737:chemistry* / Q000502:physiology; D017136:Ion Transport; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000378:metabolism; D011312:Pressure; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013314:Stress, Mechanical
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D007473:Ion Channels; C086596:MscL protein, E coli