Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate
Phan, Gilles and Remaut, Han and Wang, T. and Allen, William J. and Pirker, Katharina F. and Lebedev, A. and Henderson, N.S. and Geibel, Sebastien and Volkan, E. and Yan, Jun and Kunze, M.B.A. and Pinkner, J.S. and Ford, B. and Kay, Christopher W.M. and Li, H.L. and Hultgren, S.J. and Thanassi, D.G. and Waksman, Gabriel (2011) Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate. Nature 474 (7349), pp. 49-53. ISSN 0028-0836.
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 Î²-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 Î²-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.
|Keyword(s) / Subject(s):||Adhesins, Escherichia coliCrystallization, Escherichia coli Proteins, Fimbriae Proteins, Models, Molecular Protein Binding, Protein Structure, Quaternary|
|School:||Birkbeck Schools and Departments > School of Science > Biological Sciences|
|Research Centre:||Structural Molecular Biology, Institute of (ISMB)|
|Date Deposited:||14 Nov 2011 12:23|
|Last Modified:||06 Dec 2016 10:46|
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