An ABC transporter with two periplasmic binding proteins involved in iron acquisition in Pseudomonas aeruginosa.

@article{Brillet2012AnAT,
  title={An ABC transporter with two periplasmic binding proteins involved in iron acquisition in Pseudomonas aeruginosa.},
  author={Karl Brillet and Frank Ruffenach and Hendrik Adams and Laure Journet and V{\'e}ronique Gasser and Françoise Hoegy and Laurent Guillon and M{\'e}lissa Hannauer and Adeline Page and Isabelle J Schalk},
  journal={ACS chemical biology},
  year={2012},
  volume={7 12},
  pages={
          2036-45
        }
}
Pyoverdine I is the main siderophore secreted byPseudomonas aeruginosa PAO1 to obtain access to iron. After extracellular iron chelation, pyoverdine-Fe uptake into the bacteria involves a specific outer-membrane transporter, FpvA. Iron is then released in the periplasm by a mechanism involving no siderophore modification but probably iron reduction. The proteins involved in this dissociation step are currently unknown. The pyoverdine locus contains the fpvCDEF operon, which contains four genes… CONTINUE READING
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