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 () and James H. Naismith ()
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Lucile Moynié: Wellcome Trust Centre of Human Genomics
Stefan Milenkovic: University of Cagliari, Cittadella Universitaria
Gaëtan L. A. Mislin: Université de Strasbourg, UMR7242, ESBS, Bld Sébastien Brant
Véronique Gasser: Université de Strasbourg, UMR7242, ESBS, Bld Sébastien Brant
Giuliano Malloci: University of Cagliari, Cittadella Universitaria
Etienne Baco: Université de Strasbourg, UMR7242, ESBS, Bld Sébastien Brant
Rory P. McCaughan: The University of St Andrews
Malcolm G. P. Page: Department of Life Sciences & Chemistry
Isabelle J. Schalk: Université de Strasbourg, UMR7242, ESBS, Bld Sébastien Brant
Matteo Ceccarelli: University of Cagliari, Cittadella Universitaria
James H. Naismith: Wellcome Trust Centre of Human Genomics

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: Abstract 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.

Date: 2019
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DOI: 10.1038/s41467-019-11508-y

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