Title | Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate. |
Publication Type | Journal Article |
Year of Publication | 2011 |
Authors | Phan, G., H. Remaut, T. Wang, W. J. Allen, K. F. Pirker, A. Lebedev, N. S. Henderson, S. Geibel, E. Volkan, J. Yan, M. B. A. Kunze, J. S. Pinkner, B. Ford, C. W. M. Kay, H. Li, S. J. Hultgren, D. G. Thanassi, and G. Waksman |
Journal | Nature |
Volume | 474 |
Issue | 7349 |
Pagination | 49-53 |
Date Published | 2011 Jun 2 |
Type of Article | smm |
ISSN | 1476-4687 |
Keywords | Adhesins, Escherichia coli, Crystallization, Escherichia coli Proteins, Fimbriae Proteins, Models, Molecular, Protein Binding, Protein Structure, Quaternary |
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. |
DOI | 10.1038/nature10109 |
Alternate Journal | Nature |
PubMed ID | 21637253 |
PubMed Central ID | PMC3162478 |
Grant List | 29549 / / PHS HHS / United States 48689 / / PHS HHS / United States 49950 / / PHS HHS / United States 85602 / / Medical Research Council / United Kingdom G0100442 / / Medical Research Council / United Kingdom G0100442(58149) / / Medical Research Council / United Kingdom GM62987 / GM / NIGMS NIH HHS / United States GM74985 / GM / NIGMS NIH HHS / United States P30 EB009998 / EB / NIBIB NIH HHS / United States R01 GM062987 / GM / NIGMS NIH HHS / United States |
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