Hospenthal, M.K. and Redzej, A. and Dodson, K. and Ukleja, M. and Frenz, B. and Rodrigues, C. and Hultgren, S.J. and DiMaio, F. and Egelman, E.H. and Waksman, Gabriel (2016) Structure of a Chaperone-Usher Pilus reveals the molecular basis of rod uncoiling. Cell 164 , pp. 269-278. ISSN 0092-8674.
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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.
Metadata
| Item Type: | Article |
|---|---|
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Structural Molecular Biology, Institute of (ISMB) |
| Depositing User: | Administrator |
| Date Deposited: | 07 Jan 2016 10:46 |
| Last Modified: | 17 Jul 2025 01:24 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/13913 |
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