Abstract
Type 1 pili, anchored to the outer membrane protein FimD, enable uropathogenic Escherichia coli to attach to host cells. During pilus biogenesis, the N-terminal periplasmic domain of FimD (FimD(N)) binds complexes between the chaperone FimC and pilus subunits via its partly disordered N-terminal segment, as recently shown for the FimC-FimH(P)-FimD(N) ternary complex. We report the structure of a new ternary complex (FimC-FimF(t)-FimD(N)) with the subunit FimF(t) instead of FimH(p). FimD(N) recognizes FimC-FimF(t) and FimC-FimH(P) very similarly, predominantly through hydrophobic interactions. The conserved binding mode at a "hot spot" on the chaperone surface could guide the design of pilus assembly inhibitors.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adhesins, Escherichia coli / chemistry
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Adhesins, Escherichia coli / metabolism
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Conserved Sequence
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Crystallography, X-Ray
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Escherichia coli / metabolism*
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / metabolism
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Fimbriae Proteins / chemistry*
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Fimbriae Proteins / metabolism
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Fimbriae, Bacterial / metabolism*
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Molecular Chaperones / metabolism*
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Multiprotein Complexes / chemistry*
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Subunits / chemistry
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Protein Subunits / metabolism
Substances
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Adhesins, Escherichia coli
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Escherichia coli Proteins
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FimF protein, E coli
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Molecular Chaperones
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Multiprotein Complexes
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Protein Subunits
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fimC protein, E coli
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fimD protein, E coli
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fimH protein, E coli
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Fimbriae Proteins