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X-ray Structure of the FimC-FimH Chaperone-Adhesin Complex from Uropathogenic Escherichia coli

Science  13 Aug 1999:
Vol. 285, Issue 5430, pp. 1061-1066
DOI: 10.1126/science.285.5430.1061

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Abstract

Type 1 pili—adhesive fibers expressed in most members of the Enterobacteriaceae family—mediate binding to mannose receptors on host cells through the FimH adhesin. Pilus biogenesis proceeds by way of the chaperone/usher pathway. The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly. The carboxyl-terminal pilin domain of FimH has an immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand complementation mechanism in which the chaperone donates a strand to complete the pilin domain explains the basis for both chaperone function and pilus biogenesis.

  • * To whom correspondence should be addressed. E-mail: hultgren{at}borcim.wustl.edu (S.J.H.); stefan{at}xray.bmc.uu.se(S.D.K.).

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