Journal article
Crystal structure of the FimD usher bound to its cognate FimC:FimH substrate
Nature (London), Vol.474(7349), pp.49-53
06/02/2011
DOI: 10.1038/nature10109
PMCID: PMC3162478
PMID: 21637253
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 catalyzes their polymerization and mediates pilus translocation across the outer membrane. 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 C-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 dramatic conformational change in the β-barrel. The N-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.
Details
- Title: Subtitle
- Crystal structure of the FimD usher bound to its cognate FimC:FimH substrate
- Creators
- Gilles Phan - Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London, WC1E 7HX, UKHan Remaut - Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London, WC1E 7HX, UKTao Wang - Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USAWilliam J Allen - Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London, WC1E 7HX, UKKatharina F Pirker - Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London, WC1E 7HX, UKAndrey Lebedev - Department of Chemistry, University of York, York, YO10 5YW, UKNadine S Henderson - Center for Infectious Diseases and Department of Molecular Genetics & Microbiology, Stony Brook University, Stony Brook, NY 11794, USASebastian Geibel - Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London, WC1E 7HX, UKEnder Volkan - Department of Molecular Microbiology and Center for Women’s Infectious Disease Research, Washington University School of Medicine, Saint Louis, MO63110, USAJun Yan - Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London, WC1E 7HX, UKMicha B.A Kunze - Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London, WC1E 7HX, UKJerome S Pinkner - Department of Molecular Microbiology and Center for Women’s Infectious Disease Research, Washington University School of Medicine, Saint Louis, MO63110, USABradley Ford - Department of Molecular Microbiology and Center for Women’s Infectious Disease Research, Washington University School of Medicine, Saint Louis, MO63110, USAChristopher W. M Kay - Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London, WC1E 7HX, UKHuilin Li - Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USAScott Hultgren - Department of Molecular Microbiology and Center for Women’s Infectious Disease Research, Washington University School of Medicine, Saint Louis, MO63110, USADavid G Thanassi - Center for Infectious Diseases and Department of Molecular Genetics & Microbiology, Stony Brook University, Stony Brook, NY 11794, USAGabriel Waksman - Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London, WC1E 7HX, UK
- Resource Type
- Journal article
- Publication Details
- Nature (London), Vol.474(7349), pp.49-53
- DOI
- 10.1038/nature10109
- PMID
- 21637253
- PMCID
- PMC3162478
- NLM abbreviation
- Nature
- ISSN
- 0028-0836
- eISSN
- 1476-4687
- Grant note
- G0100442(58149) || MRC_ / Medical Research Council :
- Language
- English
- Date published
- 06/02/2011
- Academic Unit
- Pathology
- Record Identifier
- 9984047695302771
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