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Crystal structure of the ternary FimC–FimF t –FimD N complex indicates conserved pilus chaperone–subunit complex recognition by the usher FimD
Author(s) -
Eidam Oliv,
Dworkowski Florian S.N.,
Glockshuber Rudi,
Grütter Markus G.,
Capitani Guido
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.01.030
Subject(s) - chaperone (clinical) , periplasmic space , protein subunit , pilus , chemistry , ternary complex , biogenesis , ternary operation , escherichia coli , microbiology and biotechnology , biochemistry , crystallography , biology , enzyme , gene , medicine , pathology , computer science , programming language
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.