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

DOI: 10.1038/s41467-019-11508-y DOI Help

Authors: Lucile Moynie (Wellcome Trust Centre of Human Genomics; The Research Complex at Harwell; The Rosalind Franklin Institute) , Stefan Milenkovic (University of Cagliari) , Gaëtan L. A. Mislin (Université de Strasbourg; CNRS) , Véronique Gasser (Université de Strasbourg; CNRS) , Giuliano Malloci (University of Cagliari) , Etienne Baco (Université de Strasbourg; CNRS) , Rory P. Mccaughan (The University of St Andrews) , Malcolm G. P. Page (Jacobs University Bremen WebsiteDirections Save) , Isabelle J. Schalk (Université de Strasbourg; Cittadella Universitaria) , Matteo Ceccarelli (University of Cagliari; Istituto Officina dei Materiali-CNR) , James H. Naismith (Wellcome Trust Centre of Human Genomics; The Research Complex at Harwell; The Rosalind Franklin Institute)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 10

State: Published (Approved)
Published: August 2019

Open Access Open Access

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.

Journal Keywords: Bacterial structural biology; Biochemistry; X-ray crystallography

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Membrane Protein Laboratory (MPL)
Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography