title: 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.
authors.affiliation: Department of Molecular Biology, Uppsala Biomedical Center, Swedish University of Agricultural Sciences, Box 590, S-753 24 Uppsala, Sweden.
authors.forename: D
authors.initials: D
authors.lastname: Choudhury
authors.forename: A
authors.initials: A
authors.lastname: Thompson
authors.forename: V
authors.initials: V
authors.lastname: Stojanoff
authors.forename: S
authors.initials: S
authors.lastname: Langermann
authors.forename: J
authors.initials: J
authors.lastname: Pinkner
authors.forename: S J
authors.initials: SJ
authors.lastname: Hultgren
authors.forename: S D
authors.initials: SD
authors.lastname: Knight
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry* / Q000378:metabolism; D018830:Adhesins, Escherichia coli; D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins; D002747:Chlorpropamide / Q000031:analogs & derivatives / Q000378:metabolism; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism / Q000472:pathogenicity; D029968:Escherichia coli Proteins; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D006860:Hydrogen Bonding; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D016415:Sequence Alignment
chemical_list: D018829:Adhesins, Bacterial; D018830:Adhesins, Escherichia coli; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; C120850:cyclohexylbutanoyl-N-hydroxyethylglucamide; C489721:fimC protein, E coli; C058769:fimH protein, E coli; D036781:Fimbriae Proteins; D002747:Chlorpropamide