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• W2085190522 endingPage "e1000617" @default.
• W2085190522 startingPage "e1000617" @default.
• W2085190522 abstract "There is increasing evidence that the catch bond mechanism, where binding becomes stronger under tensile force, is a common property among non-covalent interactions between biological molecules that are exposed to mechanical force in vivo. Here, by using the multi-protein tip complex of the mannose-binding type 1 fimbriae of Escherichia coli, we show how the entire quaternary structure of the adhesive organella is adapted to facilitate binding under mechanically dynamic conditions induced by flow. The fimbrial tip mediates shear-dependent adhesion of bacteria to uroepithelial cells and demonstrates force-enhanced interaction with mannose in single molecule force spectroscopy experiments. The mannose-binding, lectin domain of the apex-positioned adhesive protein FimH is docked to the anchoring pilin domain in a distinct hooked manner. The hooked conformation is highly stable in molecular dynamics simulations under no force conditions but permits an easy separation of the domains upon application of an external tensile force, allowing the lectin domain to switch from a low- to a high-affinity state. The conformation between the FimH pilin domain and the following FimG subunit of the tip is open and stable even when tensile force is applied, providing an extended lever arm for the hook unhinging under shear. Finally, the conformation between FimG and FimF subunits is highly flexible even in the absence of tensile force, conferring to the FimH adhesin an exploratory function and high binding rates. The fimbrial tip of type 1 Escherichia coli is optimized to have a dual functionality: flexible exploration and force sensing. Comparison to other structures suggests that this property is common in unrelated bacterial and eukaryotic adhesive complexes that must function in dynamic conditions." @default.
• W2085190522 created "2016-06-24" @default.
• W2085190522 creator A5007117025 @default.
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• W2085190522 date "2011-05-10" @default.
• W2085190522 modified "2023-10-14" @default.
• W2085190522 title "The Bacterial Fimbrial Tip Acts as a Mechanical Force Sensor" @default.
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• W2085190522 doi "https://doi.org/10.1371/journal.pbio.1000617" @default.
• W2085190522 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3091844" @default.
• W2085190522 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21572990" @default.
• W2085190522 hasPublicationYear "2011" @default.
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