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3bwu
From Proteopedia
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Crystal structure of the ternary complex of FimD (N-Terminal Domain, FimDN) with FimC and the N-terminally truncated pilus subunit FimF (FimFt)
Overview
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.
About this Structure
3BWU is a Protein complex structure of sequences from Escherichia coli with and as ligands. Known structural/functional Sites: , , , , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Mar 5 13:24:26 2008
