Structure and function of the bacterial mechanosensitive channel of large conductance

Protein Sci. 1999 Oct;8(10):1915-21. doi: 10.1110/ps.8.10.1915.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Escherichia coli Proteins*
  • Ion Channel Gating
  • Ion Channels / chemistry*
  • Ion Channels / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Mycobacterium tuberculosis / chemistry
  • Protein Conformation
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Ion Channels
  • MscL protein, E coli