3BWU

Crystal structure of the ternary complex of FimD (N-Terminal Domain, FimDN) with FimC and the N-terminally truncated pilus subunit FimF (FimFt)

Summary for 3BWU

• Entry DOI: 10.2210/pdb3bwu/pdb
• Related: 1ZE3
• Descriptor: Chaperone protein fimC, Outer membrane usher protein FimD, N-terminal domain, Protein fimF, ... (6 entities in total)
• Functional Keywords: usher, n-terminal domain, ternary complex with chaperone and pilus subunit, chaperone, structural protein, mebrane protein, structural, membrane protein
• Biological source: Escherichia coli; More
• Cellular location: Periplasm: P31697; Cell outer membrane ; Multi- pass membrane protein : P30130; Fimbrium: P08189
• Total number of polymer chains: 3
• Total formula weight: 52172.88

Authors

Eidam, O.,Grutter, M.G.,Capitani, G. (deposition date: 2008-01-10, release date: 2008-03-04, Last modification date: 2024-11-20)

Primary citation

Eidam, O.,Dworkowski, F.S.,Glockshuber, R.,Grutter, M.G.,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., 582:651-655, 2008

PubMed 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.

PubMed: 18242189
DOI: 10.1016/j.febslet.2008.01.030

Experimental method

X-RAY DIFFRACTION (1.76 Å)