Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate
Type 1 pili are the archetypal representative of a widespread class of adhesive multisubunit fibres in Gram-negative bacteria. During pilus assembly, subunits dock as chaperone-bound complexes to an usher, which catalyses their polymerization and mediates pilus translocation across the outer membrane. Here we report the crystal structure of the full-length FimD usher bound to the FimC-FimH chaperone-adhesin complex and that of the unbound form of the FimD translocation domain. The FimD-FimC-FimH structure shows FimH inserted inside the FimD 24-stranded {beta}-barrel translocation channel. FimC-FimH is held in place through interactions with the two carboxy-terminal periplasmic domains of FimD, a binding mode confirmed in solution by electron paramagnetic resonance spectroscopy. To accommodate FimH, the usher plug domain is displaced from the barrel lumen to the periplasm, concomitant with a marked conformational change in the {beta}-barrel. The amino-terminal domain of FimD is observed in an ideal position to catalyse incorporation of a newly recruited chaperone-subunit complex. The FimD-FimC-FimH structure provides unique insights into the pilus subunit incorporation cycle, and captures the first view of a protein transporter in the act of secreting its cognate substrate.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Sponsoring Organization:
- LABORATORY-DIRECTED RESEARCH AND DEVELOPMENT
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 1025493
- Report Number(s):
- BNL-95411-2011-JA; R&D Project: 10-16; YN0100000; TRN: US201120%%571
- Journal Information:
- Nature, Vol. 474, Issue 7349; ISSN 0028-0836
- Country of Publication:
- United States
- Language:
- English
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