The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action
العنوان: | The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action |
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المؤلفون: | Marie Skepö, Julia Weikum, Alina Kulakova, Jack C. Leo, Shogo Yoshimoto, J. Preben Morth, Katsutoshi Hori, Giulio Tesei, Pernille Harris, Line Vejby Jægerum, Monika Schütz |
المصدر: | Weikum, J, Kulakova, A, Tesei, G, Yoshimoto, S, Jægerum, L V, Schütz, M, Hori, K, Skepö, M, Harris, P, Leo, J C & Morth, J P 2020, ' The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action ', Scientific Reports, vol. 10, 21249 . https://doi.org/10.1038/s41598-020-77706-7 Scientific Reports Weikum, J, Vitaliyivna Kulakova, A, Tesei, G, Yoshimoto, S, Jægerum, L V, Schütz, M, Hori, K, Skepö, M, Harris, P, Leo, J C & Morth, J P 2020, ' The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action ', Scientific Reports, vol. 10, no. 1, 21249 . https://doi.org/10.1038/s41598-020-77706-7 Scientific reports 10(1), 21249 (2020). doi:10.1038/s41598-020-77706-7 |
سنة النشر: | 2020 |
مصطلحات موضوعية: | 0301 basic medicine, Virulence Factors, Mathematics and computing, 030106 microbiology, Biophysics, Biochemistry, Protein Structure, Secondary, Article, Virulence factor, Atomic force microscopy, 03 medical and health sciences, Extracellular, Enteropathogenic Escherichia coli, Adhesins, Bacterial, Biological sciences, X-ray crystallography, Juncture, Intimin, Bacterial structural biology, Multidisciplinary, Chemistry, Escherichia coli Proteins, SAXS, Cell biology, 030104 developmental biology, Mitochondrial Membranes, Molecular modelling, Pathogens, Structural biology, ddc:600, Bacterial Outer Membrane Proteins, Autotransporters |
الوصف: | Scientific reports 10(1), 21249 (2020). doi:10.1038/s41598-020-77706-7 Enterohemorrhagic and enteropathogenic Escherichia coli are among the most important food-borne pathogens, posing a global health threat. The virulence factor intimin is essential for the attachment of pathogenic E. coli to the intestinal host cell. Intimin consists of four extracellular bacterial immunoglobulin-like (Big) domains, D00–D2, extending into the fifth lectin subdomain (D3) that binds to the Tir-receptor on the host cell. Here, we present the crystal structures of the elusive D00–D0 domains at 1.5 Å and D0–D1 at 1.8 Å resolution, which confirms that the passenger of intimin has five distinct domains. We describe that D00–D0 exhibits a higher degree of rigidity and D00 likely functions as a juncture domain at the outer membrane-extracellular medium interface. We conclude that D00 is a unique Big domain with a specific topology likely found in a broad range of other inverse autotransporters. The accumulated data allows us to model the complete passenger of intimin and propose functionality to the Big domains, D00–D0–D1, extending directly from the membrane. Published by Macmillan Publishers Limited, part of Springer Nature, [London] |
وصف الملف: | application/pdf |
اللغة: | English |
تدمد: | 2045-2322 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::023c209e29fde8baa2495ee27655d3c8 https://curis.ku.dk/portal/da/publications/the-extracellular-juncture-domains-in-the-intimin-passenger-adopt-a-constitutively-extended-conformation-inducing-restraints-to-its-sphere-of-action(e47b40d1-c894-4780-a8ae-3aaf17436d9c).html |
حقوق: | OPEN |
رقم الأكسشن: | edsair.doi.dedup.....023c209e29fde8baa2495ee27655d3c8 |
قاعدة البيانات: | OpenAIRE |
تدمد: | 20452322 |
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