Abstract
Pili permit uropathogenic Escherichia coli to adhere to, and colonize, host tissues. P pili consist of a rod of PapA subunits connected to a tip fibrillum by a PapK adaptor. Type I pili are also composite structures, with a short tip fibrillum, composed of FimG and the FimH adhesin, joined to a FimA rod. Two parallel studies 1 Sauer F.G. et al. Structural basis of chaperone function and pilus biogenesis. Science. 1999; 285: 1058-1061 Crossref PubMed Scopus (327) Google Scholar , 2 Choudhury D. et al. X-ray structure of the FimC–FimH chaperone–adhesin complex from uropathogenic Escherichia coli. Science. 1999; 285: 1061-1066 Crossref PubMed Scopus (517) Google Scholar published in Science report the crystal structure of complexes between different chaperones and pilin subunits and model the molecular events in pilus biogenesis. They also illustrate how chaperones influence protein folding by protecting virgin (newly made) proteins and preventing non-productive interactions.
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