期刊
FEBS LETTERS
卷 582, 期 5, 页码 651-655出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.01.030
关键词
type 1 pilus; outer membrane usher; FimD; chaperone-subunit complex; macromolecular recognition
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). FimDN 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. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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