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Science 13 August 1999: Vol. 285. no. 5430, pp. 1061 - 1066 DOI: 10.1126/science.285.5430.1061
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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.).
Read the Full Text
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281, 14644-14653
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- W. Thomas, M. Forero, O. Yakovenko, L. Nilsson, P. Vicini, E. Sokurenko, and V. Vogel (2006)
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- M. J. Duncan, E. L. Mann, M. S. Cohen, I. Ofek, N. Sharon, and S. N. Abraham (2005)
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