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Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling
Author(s) -
Manuela K. Hospenthal,
Adam Redzej,
Karen Dodson,
Marta Ukleja,
Brandon Frenz,
Catarina A. B. Rodrigues,
Scott J. Hultgren,
Frank DiMaio,
Edward H. Egelman,
Gabriel Waksman
Publication year - 2015
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2015.11.049
Subject(s) - biology , pilus , chaperone (clinical) , genetics , escherichia coli , gene , medicine , pathology
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.

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