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Multidrug-exporting secondary transporters.

Satoshi Murakami1, Akihito Yamaguchi

  • 1Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, 567-0047, Osaka, Japan. mura@sanken.osaka-u.ac.jp

Current Opinion in Structural Biology
|September 2, 2003
PubMed
Summary

Gram-negative bacteria resist drugs using multidrug exporters like AcrB, which pump substances out of the cell. A crystal structure reveals AcrB

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Intrinsic drug resistance in Gram-negative bacteria is a significant clinical challenge.
  • Multidrug exporters are key to this resistance, facilitating drug efflux from bacterial cells.

Purpose of the Study:

  • To elucidate the mechanism of multidrug export mediated by resistance nodulation division (RND) type exporters.
  • To analyze the structural features of the AcrB multidrug exporter from Escherichia coli.

Main Methods:

  • Determination of the crystal structure of the AcrB trimer.
  • Analysis of the structural components involved in substrate transport.

Main Results:

  • The AcrB trimer possesses three periplasmic vestibules at the headpiece-transmembrane interface.

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  • Substrates access the central cavity from the cytoplasmic membrane and are transported through an extramembrane pore to the TolC channel.

    • Conclusions:

    • The crystal structure provides detailed insights into the AcrB-mediated multidrug export mechanism.
    • Understanding this mechanism is crucial for developing strategies to combat bacterial drug resistance.