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Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling
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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cell Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4715182/ https://www.ncbi.nlm.nih.gov/pubmed/26724865 http://dx.doi.org/10.1016/j.cell.2015.11.049 |
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author | Hospenthal, Manuela K. Redzej, Adam Dodson, Karen Ukleja, Marta Frenz, Brandon Rodrigues, Catarina Hultgren, Scott J. DiMaio, Frank Egelman, Edward H. Waksman, Gabriel |
author_facet | Hospenthal, Manuela K. Redzej, Adam Dodson, Karen Ukleja, Marta Frenz, Brandon Rodrigues, Catarina Hultgren, Scott J. DiMaio, Frank Egelman, Edward H. Waksman, Gabriel |
author_sort | Hospenthal, Manuela K. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4715182 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Cell Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-47151822016-02-12 Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling Hospenthal, Manuela K. Redzej, Adam Dodson, Karen Ukleja, Marta Frenz, Brandon Rodrigues, Catarina Hultgren, Scott J. DiMaio, Frank Egelman, Edward H. Waksman, Gabriel Cell Article 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. Cell Press 2016-01-14 /pmc/articles/PMC4715182/ /pubmed/26724865 http://dx.doi.org/10.1016/j.cell.2015.11.049 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Hospenthal, Manuela K. Redzej, Adam Dodson, Karen Ukleja, Marta Frenz, Brandon Rodrigues, Catarina Hultgren, Scott J. DiMaio, Frank Egelman, Edward H. Waksman, Gabriel Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling |
title | Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling |
title_full | Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling |
title_fullStr | Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling |
title_full_unstemmed | Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling |
title_short | Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling |
title_sort | structure of a chaperone-usher pilus reveals the molecular basis of rod uncoiling |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4715182/ https://www.ncbi.nlm.nih.gov/pubmed/26724865 http://dx.doi.org/10.1016/j.cell.2015.11.049 |
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