The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc.

@article{Ilari2014TheSE,
  title={The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc.},
  author={Andrea Ilari and Flaminia Alaleona and Giancarlo Tria and Patrizia Petrarca and Andrea Battistoni and Carlotta Zamparelli and Daniela Verzili and Mattia Falconi and Emilia Chiancone},
  journal={Biochimica et biophysica acta},
  year={2014},
  volume={1840 1},
  pages={535-44}
}
BACKGROUND In Gram-negative bacteria the ZnuABC transporter ensures adequate zinc import in Zn(II)-poor environments, like those encountered by pathogens within the infected host. Recently, the metal-binding protein ZinT was suggested to operate as an accessory component of ZnuABC in periplasmic zinc recruitment. Since ZinT is known to form a ZinT-ZnuA complex in the presence of Zn(II) it was proposed to transfer Zn(II) to ZnuA. The present work was undertaken to test this claim. METHODS ZinT… CONTINUE READING

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