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• W2149461468 abstract "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 FimD usher bound to the FimC–FimH chaperone–adhesin complex and that of the unbound form of the FimD translocation domain. The FimD–FimC–FimH structure shows FimH inserted inside the FimD 24-stranded β-barrel translocation channel. FimC–FimH is held in place through interactions with the two carboxy-terminal periplasmic domains of FimD, a binding mode confirmed in solution by electron paramagnetic resonance spectroscopy. To accommodate FimH, the usher plug domain is displaced from the barrel lumen to the periplasm, concomitant with a marked conformational change in the β-barrel. The amino-terminal domain of FimD is observed in an ideal position to catalyse incorporation of a newly recruited chaperone–subunit complex. The FimD–FimC–FimH structure provides unique insights into the pilus subunit incorporation cycle, and captures the first view of a protein transporter in the act of secreting its cognate substrate. Gram-negative bacteria express appendages known as pili on their outer surfaces that are used for attachment and invasion of host cells. The chaperone–usher pili are assembled at the outer membrane by a periplasmic chaperone and an outer-membrane, pore-forming protein called the usher. Gabriel Waksman and colleagues present a high-resolution crystal structure of the usher (FimD) from uropathogenic Escherichia coli bound to a translocating substrate (FimH adhesin). The structure provides insight into the activation mechanism of an archetypal protein transporter, and may inform the design of drugs capable of disrupting type 1 pilus formation and potentially inhibiting cystitis." @default.
• W2149461468 created "2016-06-24" @default.
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• W2149461468 date "2011-06-01" @default.
• W2149461468 modified "2023-09-26" @default.
• W2149461468 title "Crystal structure of the FimD usher bound to its cognate FimC–FimH substrate" @default.
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• W2149461468 doi "https://doi.org/10.1038/nature10109" @default.
• W2149461468 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3162478" @default.
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• W2149461468 hasPublicationYear "2011" @default.
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