1QUN

X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI

Summary for 1QUN

• Entry DOI: 10.2210/pdb1qun/pdb
• Descriptor: PAPD-LIKE CHAPERONE FIMC, MANNOSE-SPECIFIC ADHESIN FIMH (3 entities in total)
• Functional Keywords: chaperone adhesin donor strand complementation, chaperone-structural protein complex, chaperone/structural protein
• Biological source: Escherichia coli; More
• Cellular location: Periplasm: P31697; Fimbrium: P08191
• Total number of polymer chains: 16
• Total formula weight: 414202.70

Authors

Choudhury, D.,Thompson, A.,Stojanoff, V.,Langerman, S.,Pinkner, J.,Hultgren, S.J.,Knight, S. (deposition date: 1999-07-01, release date: 1999-08-31, Last modification date: 2011-07-13)

Primary citation

Choudhury, D.,Thompson, A.,Stojanoff, V.,Langermann, S.,Pinkner, J.,Hultgren, S.J.,Knight, S.D.
X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli.
Science, 285:1061-1066, 1999

PubMed 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: 10446051
DOI: 10.1126/science.285.5430.1061

Experimental method

X-RAY DIFFRACTION (2.8 Å)