Hospenthal, MK; Redzej, A; Dodson, K; Ukleja, M; Frenz, B; Rodrigues, C; Hultgren, SJ; ... Waksman, G; + view all Hospenthal, MK; Redzej, A; Dodson, K; Ukleja, M; Frenz, B; Rodrigues, C; Hultgren, SJ; DiMaio, F; Egelman, EH; Waksman, G; - view fewer (2016) Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling. Cell , 164 (1-2) pp. 269-278. 10.1016/j.cell.2015.11.049.

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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.

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