The complex of ferric-enterobactin with its transporter from Pseudomonas aeruginosa suggests a two-site model.

Lucile Moynié, Stefan Milenkovic, Gaëtan L A Mislin, Véronique Gasser, Giuliano Malloci, Etienne Baco, Rory P McCaughan, Malcolm G P Page, Isabelle J Schalk, Matteo Ceccarelli, James H Naismith

Nature communications 2019 Aug 14

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Bacteria use small molecules called siderophores to scavenge iron. Siderophore-Fe3+ complexes are recognised by outer-membrane transporters and imported into the periplasm in a process dependent on the inner-membrane protein TonB. The siderophore enterobactin is secreted by members of the family Enterobacteriaceae, but many other bacteria including Pseudomonas species can use it. Here, we show that the Pseudomonas transporter PfeA recognises enterobactin using extracellular loops distant from the pore. The relevance of this site is supported by in vivo and in vitro analyses. We suggest there is a second binding site deeper inside the structure and propose that correlated changes in hydrogen bonds link binding-induced structural re-arrangements to the structural adjustment of the periplasmic TonB-binding motif.

Citation

Lucile Moynié, Stefan Milenkovic, Gaëtan L A Mislin, Véronique Gasser, Giuliano Malloci, Etienne Baco, Rory P McCaughan, Malcolm G P Page, Isabelle J Schalk, Matteo Ceccarelli, James H Naismith. The complex of ferric-enterobactin with its transporter from Pseudomonas aeruginosa suggests a two-site model. Nature communications. 2019 Aug 14;10(1):3673