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Cell. 2016 Jan 14;164(1-2):269-278. doi: 10.1016/j.cell.2015.11.049. Epub 2015 Dec 24.

Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling.

Author information

1
Institute of Structural and Molecular Biology, University College London and Birkbeck, Malet Street, London, WC1E 7HX, UK.
2
Center for Women's Infectious Disease Research and Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63011, USA.
3
Department of Biochemistry, University of Washington, Seattle, WA 98105, USA.
4
Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22901, USA. Electronic address: egelman@virginia.edu.
5
Institute of Structural and Molecular Biology, University College London and Birkbeck, Malet Street, London, WC1E 7HX, UK. Electronic address: g.waksman@mail.cryst.bbk.ac.uk.

Abstract

Types 1 and P pili are prototypical bacterial cell-surface appendages playing essential roles in mediating adhesion of bacteria to the urinary tract. These pili, assembled by the chaperone-usher pathway, are polymers of pilus subunits assembling into two parts: a thin, short tip fibrillum at the top, mounted on a long pilus rod. The rod adopts a helical quaternary structure and is thought to play essential roles: its formation may drive pilus extrusion by preventing backsliding of the nascent growing pilus within the secretion pore; the rod also has striking spring-like properties, being able to uncoil and recoil depending on the intensity of shear forces generated by urine flow. Here, we present an atomic model of the P pilus generated from a 3.8 Å resolution cryo-electron microscopy reconstruction. This structure provides the molecular basis for the rod's remarkable mechanical properties and illuminates its role in pilus secretion.

PMID:
26724865
PMCID:
PMC4715182
DOI:
10.1016/j.cell.2015.11.049
[Indexed for MEDLINE]
Free PMC Article

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