Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling.
Cell
; 164(1-2): 269-278, 2016 Jan 14.
Article
in En
| MEDLINE
| ID: mdl-26724865
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.
Full text:
1
Database:
MEDLINE
Main subject:
Fimbriae, Bacterial
/
Escherichia coli Proteins
/
Uropathogenic Escherichia coli
Language:
En
Year:
2016
Type:
Article