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Science 13 August 1999:
Vol. 285. no. 5430, pp. 1061 - 1066
DOI: 10.1126/science.285.5430.1061

Reports

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

Devapriya Choudhury, 1 Andrew Thompson, 2 Vivian Stojanoff, 3 Solomon Langermann, 4 Jerome Pinkner, 5 Scott J. Hultgren, 5* Stefan D. Knight 1*

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.

1 Department of Molecular Biology, Uppsala Biomedical Center, Swedish University of Agricultural Sciences, Box 590, S-753 24 Uppsala, Sweden.
2 European Molecular Biology Laboratory Grenoble Outstation, c/o Avenue des Martyrs, BP 156X, 38042 Grenoble, France.
3 European Synchrotron Radiation Facility, Avenue des Martyrs, 38400 Grenoble, France.
4 MedImmune, Gaithersburg, MD 20878, USA.
5 Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA.
*   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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Science. ISSN 0036-8075 (print), 1095-9203 (online)