Structures of intermediate transport states of ZneA, a Zn(II)/proton antiporter.

@article{Pak2013StructuresOI,
  title={Structures of intermediate transport states of ZneA, a Zn(II)/proton antiporter.},
  author={John Edward Pak and Elisabeth Ngonlong Ekend{\'e} and Efrem G Kifle and Joseph Daniel O'Connell and Fabien De Angelis and Meseret B Tessema and Kheiro-Mouna Derfoufi and Yaneth Robles-Colmenares and Rebecca A. Robbins and Erik Goormaghtigh and Guy Vandenbussche and Robert Michael Stroud},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 46},
  pages={18484-9}
}
Efflux pumps belonging to the ubiquitous resistance-nodulation-cell division (RND) superfamily transport substrates out of cells by coupling proton conduction across the membrane to a conformationally driven pumping cycle. The heavy metal-resistant bacteria Cupriavidus metallidurans CH34 relies notably on as many as 12 heavy metal efflux pumps of the RND superfamily. Here we show that C. metallidurans CH34 ZneA is a proton driven efflux pump specific for Zn(II), and that transport of substrates… CONTINUE READING

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