5FLU

Structure of a Chaperone-Usher pilus reveals the molecular basis of rod uncoilin

Summary for 5FLU

• Entry DOI: 10.2210/pdb5flu/pdb
• EMDB information: 3222
• Descriptor: PAP FIMBRIAL MAJOR PILIN PROTEIN (1 entity in total)
• Functional Keywords: structural protein, helical polymer, strand donation
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 13
• Total formula weight: 215388.50

Authors

Hospenthal, M.K.,Redzej, A.,Dodson, K.,Ukleja, M.,Frenz, B.,Hultgren, S.J.,DiMaio, F.,Egelman, E.H.,Waksman, G. (deposition date: 2015-10-28, release date: 2016-01-13, Last modification date: 2024-10-16)

Primary citation

Hospenthal, M.K.,Redzej, A.,Dodson, K.,Ukleja, M.,Frenz, B.,Rodrigues, C.,Hultgren, S.J.,Dimaio, F.,Egelman, E.H.,Waksman, G.
Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling.
Cell(Cambridge,Mass.), 164:269-, 2016

PubMed 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.

PubMed: 26724865
DOI: 10.1016/J.CELL.2015.11.049

Experimental method

ELECTRON MICROSCOPY (3.8 Å)