Conserved low-affinity nickel-binding amino acids are essential for the function of the nickel permease NixA of Helicobacter pylori.

@article{Wolfram2002ConservedLN,
  title={Conserved low-affinity nickel-binding amino acids are essential for the function of the nickel permease NixA of Helicobacter pylori.},
  author={Laurissa J Wolfram and Peter Bauerfeind},
  journal={Journal of bacteriology},
  year={2002},
  volume={184 5},
  pages={
          1438-43
        }
}
Nickel acquisition is necessary for urease activity, a major virulence factor of the human gastric pathogen Helicobacter pylori. The nickel permease NixA of H. pylori is a member of the single-component nickel-cobalt transporter family. To identify functionally relevant amino acids of NixA, single-site exchanges were introduced into NixA via PCR-based mutagenesis. This study investigated one of the recognition motifs for this family in transmembrane segment III and other conserved amino acids… CONTINUE READING

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