Journal
NATURE
Volume 474, Issue 7349, Pages 49-U71Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature10109
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Funding
- Medical Research Council [85602]
- NIH [GM62987, 49950, 29549, 48689, GM74985]
- BNL [10-16]
- VIB
- FWO-Vlaanderen
- Austrian Science Fund [J 2959-N17]
- Biotechnology and Biological Sciences Research Council [BB/F001134/1] Funding Source: researchfish
- Medical Research Council [G0100442, G0800002] Funding Source: researchfish
- BBSRC [BB/F001134/1] Funding Source: UKRI
- MRC [G0800002, G0100442] Funding Source: UKRI
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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.
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