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Channel-tunnels.

V Koronakis1, C Andersen, C Hughes

  • 1Department of Pathology, Cambridge University, Tennis Court Road, Cambridge CB2 1QP, UK. vk103@mole.bio.cam.ac.uk

Current Opinion in Structural Biology
|August 10, 2001
PubMed
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TolC proteins form a channel in bacterial outer membranes for substrate export. This channel opens via an iris-like mechanism when interacting with specific proteins.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • TolC and its homologues are essential outer membrane proteins in bacteria.
  • These proteins form a transperiplasmic tunnel facilitating the efflux of various substrates.
  • The structure involves an alpha-helical tunnel connected to a beta-barrel channel.

Purpose of the Study:

  • To elucidate the structural and functional mechanism of the TolC channel.
  • To understand how the periplasmic entrance of the channel is regulated.
  • To investigate the role of substrate-engaged proteins in channel opening.

Main Methods:

  • Structural analysis of TolC and related proteins.
  • Biochemical assays to study substrate binding and transport.

Related Experiment Videos

  • In vitro reconstitution of the channel and its regulatory components.
  • Main Results:

    • TolC forms a contiguous channel through the bacterial outer membrane.
    • The periplasmic entrance of the channel is typically closed.
    • An 'iris-like' mechanism opens the channel upon recruitment by cytosolic proteins.

    Conclusions:

    • TolC functions as a major bacterial efflux pump.
    • Channel gating is regulated by an iris-like mechanism at the periplasmic entrance.
    • This mechanism allows for controlled substrate export in response to cellular signals.