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Gene Review

ECs5275  -  protein FimC

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs5275

  • FimC mediates the assembly of type-1 pili, which are filamentous surface organelles of uropathogenic Escherichia coli strains that enable the bacteria to attach to host cell surfaces and persist in macrophages [1].

High impact information on ECs5275

  • During pilus assembly, FimD binds complexes between the chaperone FimC and type 1 pilus subunits in the periplasm and mediates subunit translocation to the cell surface [2].
  • 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) [3].
  • The deduced primary sequence of FimC shows a high degree of homology to PapD and fits well with the derived consensus sequence for periplasmic chaperones, predicting that it has an immunoglobulin-like topology [4].
  • Principal component analysis performed on the chemical shift perturbation data revealed the presence of three binding sites on the surface of FimC, which interacted with three different classes of pilicides [5].

Biological context of ECs5275

  • FimC thus represents a previously unknown type of protein-folding catalyst, and simultaneously acts as a kinetic trap preventing spontaneous subunit assembly in the periplasm [6].


  1. NMR solution structure of the periplasmic chaperone FimC. Pellecchia, M., Güntert, P., Glockshuber, R., Wüthrich, K. Nat. Struct. Biol. (1998) [Pubmed]
  2. Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD. Nishiyama, M., Horst, R., Eidam, O., Herrmann, T., Ignatov, O., Vetsch, M., Bettendorff, P., Jelesarov, I., Grütter, M.G., Wüthrich, K., Glockshuber, R., Capitani, G. EMBO J. (2005) [Pubmed]
  3. Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR. Pellecchia, M., Sebbel, P., Hermanns, U., Wüthrich, K., Glockshuber, R. Nat. Struct. Biol. (1999) [Pubmed]
  4. FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria. Jones, C.H., Pinkner, J.S., Nicholes, A.V., Slonim, L.N., Abraham, S.N., Hultgren, S.J. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  5. NMR studies of interactions between periplasmic chaperones from uropathogenic E. coli and pilicides that interfere with chaperone function and pilus assembly. Hedenström, M., Emtenäs, H., Pemberton, N., Aberg, V., Hultgren, S.J., Pinkner, J.S., Tegman, V., Almqvist, F., Sethson, I., Kihlberg, J. Org. Biomol. Chem. (2005) [Pubmed]
  6. Pilus chaperones represent a new type of protein-folding catalyst. Vetsch, M., Puorger, C., Spirig, T., Grauschopf, U., Weber-Ban, E.U., Glockshuber, R. Nature (2004) [Pubmed]
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