Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system.

@article{Touz2004InteractionsUA,
  title={Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system.},
  author={Thierry Touz{\'e} and Jeyanthy Eswaran and Evert Bokma and Eva Koronakis and Colin Hughes and Vassilis Koronakis},
  journal={Molecular microbiology},
  year={2004},
  volume={53 2},
  pages={697-706}
}
The major Escherichia coli multidrug efflux pump AcrAB-TolC expels a wide range of antibacterial agents. Using in vivo cross-linking, we show for the first time that the antiporter AcrB and the adaptor AcrA, which form a translocase in the inner membrane, interact with the outer membrane TolC exit duct to form a contiguous proteinaceous complex spanning the bacterial cell envelope. Assembly of the pump appeared to be constitutive, occurring in the presence and absence of drug efflux substrate… CONTINUE READING

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