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

doi:10.1038/s41467-019-11508-y

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^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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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.

Original language	English
Article number	3673
Number of pages	14
Journal	Nature Communications
Volume	10
Early online date	14 Aug 2019
DOIs	https://doi.org/10.1038/s41467-019-11508-y
Publication status	E-pub ahead of print - 14 Aug 2019

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10.1038/s41467-019-11508-yLicence: CC BY

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Final published version, 3.42 MBLicence: CC BY

Transport and Polymerisation INV Award: Transport and polymerisation of bacterial polysaccharides
Naismith, J. (PI)
The Wellcome Trust
1/07/13 → 30/06/20
Project: Standard

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Moynié, L., Milenkovic, S., Mislin, G. L. A., Gasser, V., Malloci, G., Baco, E., McCaughan, R. P., Page, M. G. P., Schalk, I. J., Ceccarelli, M., & Naismith, J. H. (2019). The complex of ferric-enterobactin with its transporter from Pseudomonas aeruginosa suggests a two-site model. Nature Communications, 10, Article 3673. Advance online publication. https://doi.org/10.1038/s41467-019-11508-y

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

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.",

author = "Lucile Moyni{\'e} and Stefan Milenkovic and Mislin, {Ga{\"e}tan L. A.} and V{\'e}ronique Gasser and Giuliano Malloci and Etienne Baco and McCaughan, {Rory P.} and Page, {Malcolm G. P.} and Schalk, {Isabelle J.} and Matteo Ceccarelli and Naismith, {James H.}",

note = "The research benefitted from support from ND4BB ENABLE Consortium has received support from the Innovative Medicines Initiatives Joint Undertaking under Grant Agreement nos. 115525 and 115583, resources which are composed of financial contribution from the European Union{\textquoteright}s seventh framework programme (FP7/ 2007–2013) and EFPIA companies in kind contribution. This is work is supported by a Wellcome Trust Investigator (100209/Z/12/Z) award. M.C. and S.M. thank the additional financial support of MIUR with the PRIN project 2015795S5W_005. I.S., G.L.A.M., V.G. and E.B. thank also Vaincre la Mucoviscidose and Association Gregory Lemarchal, French associations against cystic fibrosis for additional financial support. J.H.N. and L.M. thank the Membrane Protein Laboratory at Diamond for beam time access.",

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AU - Moynié, Lucile

AU - Milenkovic, Stefan

AU - Mislin, Gaëtan L. A.

AU - Gasser, Véronique

AU - Malloci, Giuliano

AU - Baco, Etienne

AU - McCaughan, Rory P.

AU - Page, Malcolm G. P.

AU - Schalk, Isabelle J.

AU - Ceccarelli, Matteo

AU - Naismith, James H.

N1 - The research benefitted from support from ND4BB ENABLE Consortium has received support from the Innovative Medicines Initiatives Joint Undertaking under Grant Agreement nos. 115525 and 115583, resources which are composed of financial contribution from the European Union’s seventh framework programme (FP7/ 2007–2013) and EFPIA companies in kind contribution. This is work is supported by a Wellcome Trust Investigator (100209/Z/12/Z) award. M.C. and S.M. thank the additional financial support of MIUR with the PRIN project 2015795S5W_005. I.S., G.L.A.M., V.G. and E.B. thank also Vaincre la Mucoviscidose and Association Gregory Lemarchal, French associations against cystic fibrosis for additional financial support. J.H.N. and L.M. thank the Membrane Protein Laboratory at Diamond for beam time access.

PY - 2019/8/14

Y1 - 2019/8/14

N2 - 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.

AB - 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.

U2 - 10.1038/s41467-019-11508-y

DO - 10.1038/s41467-019-11508-y

M3 - Article

SN - 2041-1723

VL - 10

JO - Nature Communications

JF - Nature Communications

M1 - 3673

ER -

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

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Transport and Polymerisation INV Award: Transport and polymerisation of bacterial polysaccharides

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