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Science 18 December 1998: Vol. 282. no. 5397, pp. 2220 - 2226 DOI: 10.1126/science.282.5397.2220
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Research Articles
Structure of the MscL Homolog from Mycobacterium tuberculosis: A Gated Mechanosensitive Ion Channel
Geoffrey Chang,
*
Robert H. Spencer,
*
Allen
T. Lee,
Margaret T. Barclay,
Douglas C. Rees
Mechanosensitive ion channels play a critical role in transducing
physical stresses at the cell membrane into an electrochemical response. The MscL family of large-conductance mechanosensitive channels is widely distributed among prokaryotes and may participate in
the regulation of osmotic pressure changes within the cell. In an
effort to better understand the structural basis for the function of
these channels, the structure of the MscL homolog from
Mycobacterium tuberculosis was determined by x-ray
crystallography to 3.5 angstroms resolution. This channel is organized
as a homopentamer, with each subunit containing two transmembrane helices and a third cytoplasmic helix. From the extracellular side,
a water-filled opening approximately 18 angstroms in diameter leads
into a pore lined with hydrophilic residues which narrows at the
cytoplasmic side to an occluded hydrophobic apex that may act as the
channel gate. This structure may serve as a model for other
mechanosensitive channels, as well as the broader class of pentameric
ligand-gated ion channels exemplified by the nicotinic acetylcholine
receptor.
Howard Hughes Medical Institute and Division of Chemistry and
Chemical Engineering, 147-75CH, California Institute of Technology,
Pasadena, CA 91125, USA.
*
These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail:
dcrees{at}caltech.edu
Read the Full Text
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- B. Martinac and O. P. Hamill (2002)
PNAS
99, 4308-4312
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- Conformational pathways in the gating of Escherichia coli mechanosensitive channel.
- Y. Kong, Y. Shen, T. E. Warth, and J. Ma (2002)
PNAS
99, 5999-6004
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