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dc.contributor.authorMoynié, Lucile
dc.contributor.authorMilenkovic, Stefan
dc.contributor.authorMislin, Gaëtan L. A.
dc.contributor.authorGasser, Véronique
dc.contributor.authorMalloci, Giuliano
dc.contributor.authorBaco, Etienne
dc.contributor.authorMcCaughan, Rory P.
dc.contributor.authorPage, Malcolm G. P.
dc.contributor.authorSchalk, Isabelle J.
dc.contributor.authorCeccarelli, Matteo
dc.contributor.authorNaismith, James H.
dc.date.accessioned2020-11-17T15:30:20Z
dc.date.available2020-11-17T15:30:20Z
dc.date.issued2019-08-14
dc.identifier.citationMoynié , 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 , vol. 10 , 3673 . https://doi.org/10.1038/s41467-019-11508-yen
dc.identifier.issn2041-1723
dc.identifier.otherPURE: 271270654
dc.identifier.otherPURE UUID: 9a1596e6-04f8-4d6b-bd60-9ed874dea49d
dc.identifier.otherJisc: 504475dcb5814d73956fa63159751fce
dc.identifier.otherpublisher-id: s41467-019-11508-y
dc.identifier.othermanuscript: 11508
dc.identifier.otherScopus: 85070779528
dc.identifier.otherWOS: 000480683300003
dc.identifier.urihttps://hdl.handle.net/10023/20995
dc.descriptionThe 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.en
dc.description.abstractBacteria 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.
dc.format.extent14
dc.language.isoeng
dc.relation.ispartofNature Communicationsen
dc.rightsCopyright © The Author(s) 2019. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.en
dc.subjectQR Microbiologyen
dc.subjectDASen
dc.subject.lccQRen
dc.titleThe complex of ferric-enterobactin with its transporter from Pseudomonas aeruginosa suggests a two-site modelen
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.identifier.doihttps://doi.org/10.1038/s41467-019-11508-y
dc.description.statusPeer revieweden
dc.identifier.grantnumber100209/Z/12/Zen


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