Structural highlights
Function
[FIMC_ECOLI] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. [FIMF_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. [FIMD_ECOLI] Involved in the export and assembly of FimA fimbrial subunits across the outer membrane.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD.,Eidam O, Dworkowski FS, Glockshuber R, Grutter MG, Capitani G FEBS Lett. 2008 Mar 5;582(5):651-5. Epub 2008 Jan 31. PMID:18242189[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Eidam O, Dworkowski FS, Glockshuber R, Grutter MG, Capitani G. Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD. FEBS Lett. 2008 Mar 5;582(5):651-5. Epub 2008 Jan 31. PMID:18242189 doi:http://dx.doi.org/10.1016/j.febslet.2008.01.030
