Crystal structure of the FimD usher bound to its cognate FimC–FimH substrate

Gilles Phan, Han Remaut, Tao Wang, William J. Allen, Katharina F. Pirker, Andrey Lebedev, Nadine S. Henderson, Sebastian Geibel, Ender Volkan, Jun Yan, Micha B. A. Kunze, Jerome S. Pinkner, Bradley Ford, Christopher W. M. Kay, Huilin Li, Scott J. Hultgren, David G. Thanassi () and Gabriel Waksman ()
Additional contact information
Gilles Phan: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Han Remaut: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Tao Wang: Brookhaven National Laboratory
William J. Allen: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Katharina F. Pirker: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Andrey Lebedev: University of York, York YO10 5YW, UK
Nadine S. Henderson: Stony Brook University
Sebastian Geibel: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Ender Volkan: Washington University School of Medicine
Jun Yan: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Micha B. A. Kunze: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Jerome S. Pinkner: Washington University School of Medicine
Bradley Ford: Washington University School of Medicine
Christopher W. M. Kay: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Huilin Li: Brookhaven National Laboratory
Scott J. Hultgren: Washington University School of Medicine
David G. Thanassi: Stony Brook University
Gabriel Waksman: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK

Nature, 2011, vol. 474, issue 7349, 49-53

Abstract: Abstract 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 β-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 β-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.

Date: 2011
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DOI: 10.1038/nature10109

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