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Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM(4−) siderophore analogues of varied linker length

Bacteria use siderophores to mediate the transport of essential Fe(III) into the cell. In Campylobacter jejuni the periplasmic binding protein CeuE, an integral part of the Fe(III) transport system, has adapted to bind tetradentate siderophores using a His and a Tyr side chain to complete the Fe(III...

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Autores principales: Wilde, Ellis J., Hughes, Adam, Blagova, Elena V., Moroz, Olga V., Thomas, Ross P., Turkenburg, Johan P., Raines, Daniel J., Duhme-Klair, Anne-Kathrin, Wilson, Keith S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5382913/
https://www.ncbi.nlm.nih.gov/pubmed/28383577
http://dx.doi.org/10.1038/srep45941
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author Wilde, Ellis J.
Hughes, Adam
Blagova, Elena V.
Moroz, Olga V.
Thomas, Ross P.
Turkenburg, Johan P.
Raines, Daniel J.
Duhme-Klair, Anne-Kathrin
Wilson, Keith S.
author_facet Wilde, Ellis J.
Hughes, Adam
Blagova, Elena V.
Moroz, Olga V.
Thomas, Ross P.
Turkenburg, Johan P.
Raines, Daniel J.
Duhme-Klair, Anne-Kathrin
Wilson, Keith S.
author_sort Wilde, Ellis J.
collection PubMed
description Bacteria use siderophores to mediate the transport of essential Fe(III) into the cell. In Campylobacter jejuni the periplasmic binding protein CeuE, an integral part of the Fe(III) transport system, has adapted to bind tetradentate siderophores using a His and a Tyr side chain to complete the Fe(III) coordination. A series of tetradentate siderophore mimics was synthesized in which the length of the linker between the two iron-binding catecholamide units was increased from four carbon atoms (4-LICAM(4−)) to five, six and eight (5-, 6-, 8-LICAM(4−), respectively). Co-crystal structures with CeuE showed that the inter-planar angles between the iron-binding catecholamide units in the 5-, 6- and 8-LICAM(4−) structures are very similar (111°, 110° and 110°) and allow for an optimum fit into the binding pocket of CeuE, the inter-planar angle in the structure of 4-LICAM(4−) is significantly smaller (97°) due to restrictions imposed by the shorter linker. Accordingly, the protein-binding affinity was found to be slightly higher for 5- compared to 4-LICAM(4−) but decreases for 6- and 8-LICAM(4−). The optimum linker length of five matches that present in natural siderophores such as enterobactin and azotochelin. Site-directed mutagenesis was used to investigate the relative importance of the Fe(III)-coordinating residues H227 and Y288.
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spelling pubmed-53829132017-04-11 Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM(4−) siderophore analogues of varied linker length Wilde, Ellis J. Hughes, Adam Blagova, Elena V. Moroz, Olga V. Thomas, Ross P. Turkenburg, Johan P. Raines, Daniel J. Duhme-Klair, Anne-Kathrin Wilson, Keith S. Sci Rep Article Bacteria use siderophores to mediate the transport of essential Fe(III) into the cell. In Campylobacter jejuni the periplasmic binding protein CeuE, an integral part of the Fe(III) transport system, has adapted to bind tetradentate siderophores using a His and a Tyr side chain to complete the Fe(III) coordination. A series of tetradentate siderophore mimics was synthesized in which the length of the linker between the two iron-binding catecholamide units was increased from four carbon atoms (4-LICAM(4−)) to five, six and eight (5-, 6-, 8-LICAM(4−), respectively). Co-crystal structures with CeuE showed that the inter-planar angles between the iron-binding catecholamide units in the 5-, 6- and 8-LICAM(4−) structures are very similar (111°, 110° and 110°) and allow for an optimum fit into the binding pocket of CeuE, the inter-planar angle in the structure of 4-LICAM(4−) is significantly smaller (97°) due to restrictions imposed by the shorter linker. Accordingly, the protein-binding affinity was found to be slightly higher for 5- compared to 4-LICAM(4−) but decreases for 6- and 8-LICAM(4−). The optimum linker length of five matches that present in natural siderophores such as enterobactin and azotochelin. Site-directed mutagenesis was used to investigate the relative importance of the Fe(III)-coordinating residues H227 and Y288. Nature Publishing Group 2017-04-06 /pmc/articles/PMC5382913/ /pubmed/28383577 http://dx.doi.org/10.1038/srep45941 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Wilde, Ellis J.
Hughes, Adam
Blagova, Elena V.
Moroz, Olga V.
Thomas, Ross P.
Turkenburg, Johan P.
Raines, Daniel J.
Duhme-Klair, Anne-Kathrin
Wilson, Keith S.
Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM(4−) siderophore analogues of varied linker length
title Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM(4−) siderophore analogues of varied linker length
title_full Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM(4−) siderophore analogues of varied linker length
title_fullStr Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM(4−) siderophore analogues of varied linker length
title_full_unstemmed Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM(4−) siderophore analogues of varied linker length
title_short Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM(4−) siderophore analogues of varied linker length
title_sort interactions of the periplasmic binding protein ceue with fe(iii) n-licam(4−) siderophore analogues of varied linker length
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5382913/
https://www.ncbi.nlm.nih.gov/pubmed/28383577
http://dx.doi.org/10.1038/srep45941
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