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Crystal structure of the FimD usher bound to its cognate FimC:FimH substrate
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 anExpand
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Domain activities of PapC usher reveal the mechanism of action of an Escherichia coli molecular machine
P pili are prototypical chaperone–usher pathway-assembled pili used by Gram-negative bacteria to adhere to host tissues. The PapC usher contains five functional domains: a transmembrane β-barrel, aExpand
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The structure of the PapD-PapGII pilin complex reveals an open and flexible P5 pocket.
P pili are hairlike polymeric structures that mediate binding of uropathogenic Escherichia coli to the surface of the kidney via the PapG adhesin at their tips. PapG is composed of two domains: aExpand
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  • Open Access
Molecular basis of usher pore gating in Escherichia coli pilus biogenesis
Significance Gram-negative bacteria use chaperone-usher pathway (CUP) pili to colonize host tissues and mediate biofilm formation. CUP ushers are outer membrane (OM) pore proteins that catalyze pilusExpand
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  • Open Access
Electrophysiological Analysis of PapC Mutants Provides Insights into the Mechanism of Plug Displacement
The PapC usher is a twin beta barrel pore of the outer membrane of uropathogenic E. coli used for the assembly of the P pilus, a key virulence factor in bacterial colonization of human kidney cells.Expand