Structure of the S pilus periplasmic chaperone SfaE at 2.2 A resolution.

@article{Knight2002StructureOT,
  title={Structure of the S pilus periplasmic chaperone SfaE at 2.2 A resolution.},
  author={Stefan D Knight and Devapriya Choudhury and Scott J Hultgren and Jerome S Pinkner and Vivian Stojanoff and Andrew V. Thompson},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2002},
  volume={58 Pt 6 Pt 2},
  pages={1016-22}
}
S pili are sialic acid binding hair-like appendages expressed by pathogenic strains of Escherichia coli. The presence of S pili has been implicated as a virulence factor in both urinary-tract infections and new-born meningitis. Assembly of S pili proceeds via the ubiquitous chaperone/usher pathway. Previously, structures of the homologous chaperones PapD and FimC involved in assembly of P and type-1 pili, respectively, have been solved. Here, the 2.2 A X-ray structure of the S pilus chaperone… CONTINUE READING