PMID:10201401

Citation	Pellecchia, M, Sebbel, P, Hermanns, U, Wüthrich, K and Glockshuber, R (1999) Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR. Nat. Struct. Biol. 6:336-9
Abstract	The 23 kDa two-domain periplasmic chaperone FimC from Escherichia coli is required for the assembly of type-1 pili, which are filamentous, highly oligomeric protein complexes anchored to the outer bacterial membrane that mediate adhesion of pathogenic E. coli strains to host cell surfaces. Here we identified the contact sites on the surface of the NMR structure of FimC that are responsible for the binding of the 28 kDa mannose-binding type-1 pilus subunit FimH by 15N and 1H NMR chemical shift mapping, using transverse relaxation-optimized spectroscopy (TROSY). The FimH-binding surface of FimC is formed nearly entirely by the N-terminal domain, and its extent and shape indicate that FimC binds a folded form of the pilus subunits.
Links	PubMed Online version:10.1038/7573
Keywords	Adhesins, Bacterial/chemistry; Adhesins, Bacterial/metabolism; Adhesins, Escherichia coli; Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/metabolism; Bacterial Proteins; Binding Sites; Escherichia coli/metabolism; Escherichia coli Proteins; Fimbriae Proteins; Fimbriae, Bacterial/chemistry; Fimbriae, Bacterial/metabolism; Models, Molecular; Molecular Sequence Data; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular/methods; Protein Conformation; Protein Folding; Surface Properties; Tritium
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