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Structure and function of the bacterial mechanosensitive channel of large conductance

Published online by Cambridge University Press:  01 October 1999

AARON J. OAKLEY ,
BORIS MARTINAC  and
MATTHEW C.J. WILCE
AARON J. OAKLEY
Affiliation:
Department of Pharmacology, University of Western Australia, Nedlands, WA 6907, Australia Crystallography Center, University of Western Australia, Nedlands, WA 6907, Australia
BORIS MARTINAC
Affiliation:
Department of Pharmacology, University of Western Australia, Nedlands, WA 6907, Australia
MATTHEW C.J. WILCE
Affiliation:
Department of Pharmacology, University of Western Australia, Nedlands, WA 6907, Australia Crystallography Center, University of Western Australia, Nedlands, WA 6907, Australia
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Abstract

Mechanosensation in bacteria involves transducing membrane stress into an electrochemical response. In Escherichia coli and other bacteria, this function is carried out by a number of proteins including MscL, the mechanosensitive channel of large conductance. MscL is the best characterized of all mechanosensitive channels. It has been the subject of numerous structural and functional investigations. The explosion in experimental data on MscL recently culminated in the solution of the three-dimensional structure of the MscL homologue from Mycobacterium tuberculosis. In this review, much of these data are united and interpreted in terms of the newly published M. tuberculosis MscL crystal structure.

Keywords

ion channelmechanosensationmechanosensitive channel of large conductancemembrane protein
Type
REVIEW
Information
Protein Science , Volume 8 , Issue 10 , October 1999 , pp. 1915 - 1921
Copyright
© 1999 The Protein Society

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