Crucial role of Asp408 in the proton translocation pathway of multidrug transporter AcrB: evidence from site-directed mutagenesis and carbodiimide labeling.

@article{Seeger2009CrucialRO,
  title={Crucial role of Asp408 in the proton translocation pathway of multidrug transporter AcrB: evidence from site-directed mutagenesis and carbodiimide labeling.},
  author={Markus A Seeger and Christoph von Ballmoos and François Verrey and Klaas M Pos},
  journal={Biochemistry},
  year={2009},
  volume={48 25},
  pages={5801-12}
}
The three-component AcrA/AcrB/TolC efflux system of Escherichia coli catalyzes the proton motive force-driven extrusion of a variety of cytotoxic compounds. The inner membrane pump component AcrB belongs to the resistance nodulation and cell division (RND) superfamily and is responsible for drug specificity and energy transduction of the entire tripartite efflux system. Systematic mutational analysis of titratable and polar membrane-located amino acids revealed four residues, D407, D408, K940… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 31 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 75 references

Similar Papers

Loading similar papers…