Skip to main page content
U.S. flag
See More

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1999 Aug 13;285(5430):1061-6.
doi: 10.1126/science.285.5430.1061.

X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli

D Choudhury  1 , A Thompson, V Stojanoff, S Langermann, J Pinkner, S J Hultgren, S D Knight
Affiliations

X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli

D Choudhury et al. Science. .

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.

PubMed Disclaimer

Comment in

Publication types

MeSH terms

Associated data

LinkOut - more resources