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Type 1 pili are the archetypal representative of a widespread class of adhesive multisubunit fibres in Gram-negative bacteria. During pilus assembly, subunits dock as chaperone-bound complexes to an usher, which catalyses their polymerization and mediates pilus translocation across the outer membrane. Here we report the crystal structure of the full-length(More)
Type 1 pili, produced by uropathogenic Escherichia coli, are multisubunit fibres crucial in recognition of and adhesion to host tissues. During pilus biogenesis, subunits are recruited to an outer membrane assembly platform, the FimD usher, which catalyses their polymerization and mediates pilus secretion. The recent determination of the crystal structure(More)
Penetratin is a short, basic cell-penetrating peptide able to induce cellular uptake of a vast variety of large, hydrophilic cargos. We have reassessed the highly controversial issue of direct permeation of the strongly cationic peptide across negatively charged lipid membranes. Confocal laser scanning microscopy on rhodamine-labeled giant vesicles(More)
PapC ushers are outer-membrane proteins enabling assembly and secretion of P pili in uropathogenic E. coli. Their translocation domain is a large β-barrel occluded by a plug domain, which is displaced to allow the translocation of pilus subunits across the membrane. Previous studies suggested that this gating mechanism is controlled by a β-hairpin and an(More)
For over five decades cell lines have taken center stage in an untold number of scientific advancements both in bio-medical research and in biotechnology. Some of the key qualities that make cell lines desirable to countless academic labs are the same attributes industry seeks such as, modeling complex biological processes, the relative ease in scaling up(More)
PapC ushers are outer-membrane proteins enabling assembly and secretion of P pili in uropathogenic E. coli. Their translocation domain is a large-barrel occluded by a plug domain, which is displaced to allow the translocation of pilus subunits across the membrane. Previous studies suggested that this gating mechanism is controlled by a-hairpin and an-helix.(More)
(2014) Allosteric signalling in the outer membrane translocation domain of PapC usher. eLife 3 , ISSN 2050-084X. and proofing. formatted HTML, PDF, and XML versions will be made available after technical processing, editing, This PDF is the version of the article that was accepted for publication after peer review. Fully unrestricted use and redistribution(More)
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