Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD |
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Authors: | Eidam Oliv Dworkowski Florian S N Glockshuber Rudi Grütter Markus G Capitani Guido |
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Institution: | University of Zurich, Department of Biochemistry, Winterthurerstrasse 190, Zurich, Switzerland. |
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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. |
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Keywords: | CFD FimC-FimFt-FimDN CHD FimC-FimHP-FimDN |
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