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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...

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Detalles Bibliográficos
Autores principales: Hospenthal, Manuela K., Redzej, Adam, Dodson, Karen, Ukleja, Marta, Frenz, Brandon, Rodrigues, Catarina, Hultgren, Scott J., DiMaio, Frank, Egelman, Edward H., Waksman, Gabriel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2016
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
Descripción
Sumario: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.