The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
X-ray Structure of the FimC-FimH Chaperone-Adhesin Complex from Uropathogenic Escherichia coli
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.
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[20] Processing of X-ray diffraction data collected in oscillation mode
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Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984
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Metadata
- Authors
- Choudhury, D., Thompson, A., Stojanoff, V., Langermann, S., Pinkner, J., Hultgren, S. J., & Knight, S. D.
- Venue
- Science
- Published
- 1999-08-13
- Volume
- 285
- Issue
- 5430
- Pages
- 1061-1066
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2115453381
- Cited by
- 610
- References
- 2
- FWCI
- 10.55
- Type
- journal article
- Language
- en
- Open access
- closed
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- Choudhury, D., Thompson, A., Stojanoff, V., Langermann, S., Pinkner, J., Hultgren, S. J., & Knight, S. D. (1999). X-ray Structure of the FimC-FimH Chaperone-Adhesin Complex from Uropathogenic Escherichia coli. Science. https://doi.org/10.1126/science.285.5430.1061
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