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Pilus chaperone FimC–adhesin FimH interactions mapped by TROSY-NMR

Nature Structural Biology volume 6, pages 336–339 (1999)Cite this article

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.

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Figure 2: a, Sequence distribution of FimC residues with large chemical shift changes upon binding to FimH.
Figure 1: Comparison of [15N,1H]-TROSY spectra2,21 of uniformly 15N,2H-labeled FimC in a, the free form and in b, the 1:1 complex with the unlabeled mannose-binding type-1 pilus subunit FimH.

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Acknowledgements

Financial support was obtained from the Schweizerischer Nationalfonds for K.W. and R.G. and from an EMBO fellowship for M.P.

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Author notes

  1. Maurizio Pellecchia

    Present address: Biophysics Research Division, The University of Michigan, 930 N. University Ave., Ann Arbor, Michigan, 48109, USA

  2. Maurizio Pellecchia and Peter Sebbel: These authors contributed equally to this work.

Authors and Affiliations

  1. Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Hönggerberg, Zürich, CH-8093, Switzerland

    Maurizio Pellecchia, Peter Sebbel, Uta Hermanns, Kurt Wüthrich & Rudi Glockshuber

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  1. Maurizio Pellecchia
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  2. Peter Sebbel
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Correspondence to Rudi Glockshuber.

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Pellecchia, M., Sebbel, P., Hermanns, U. et al. Pilus chaperone FimC–adhesin FimH interactions mapped by TROSY-NMR. Nat Struct Mol Biol 6, 336–339 (1999). https://doi.org/10.1038/7573

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