Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD.
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.
Eidam
Oliv
O
University of Zurich, Department of Biochemistry, Winterthurerstrasse 190, Zurich, Switzerland.
Dworkowski
Florian S N
FS
Glockshuber
Rudi
R
Grütter
Markus G
MG
Capitani
Guido
G
D018830:Adhesins, Escherichia coli / Q000737:chemistry / Q000378:metabolism; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D036781:Fimbriae Proteins / Q000737:chemistry* / Q000378:metabolism; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D046912:Multiprotein Complexes / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
D018830:Adhesins, Escherichia coli; D029968:Escherichia coli Proteins; C521674:FimF protein, E coli; D018832:Molecular Chaperones; D046912:Multiprotein Complexes; D021122:Protein Subunits; C489721:fimC protein, E coli; C489283:fimD protein, E coli; C058769:fimH protein, E coli; D036781:Fimbriae Proteins