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TitleStructure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling.
Journal, issue, pagesCell, Vol. 164, Issue 1-2, Page 269-278, Year 2016
Publish dateJan 14, 2016
AuthorsManuela K Hospenthal / Adam Redzej / Karen Dodson / Marta Ukleja / Brandon Frenz / Catarina Rodrigues / Scott J Hultgren / Frank DiMaio / Edward H Egelman / Gabriel Waksman /
PubMed AbstractTypes 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 ...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.
External linksCell / PubMed:26724865 / PubMed Central
MethodsEM (helical sym.)
Resolution3.8 Å
Structure data

3222

5flu

EMDB-3222, PDB-5flu:
Structure of a Chaperone-Usher pilus reveals the molecular basis of rod uncoilin
Method: EM (helical sym.) / Resolution: 3.8 Å

Source
  • escherichia coli (E. coli)
KeywordsSTRUCTURAL PROTEIN / HELICAL POLYMER / STRAND DONATION

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