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NMR solution structure of the periplasmic chaperone FimC

Nature Structural Biology volume 5, pages 885–890 (1998)Cite this article

Abstract

The NMR structure of the 205-residue periplasmic chaperone FimC is presented. This protein consists of two globular domains with immunoglobulin-like folds connected by a 15-residue linker peptide. The relative orientation of the two domains is defined by hydrophobic contacts and an interdomain salt bridge. 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. The availability of the NMR structure of FimC provides a new basis for rational design of drugs against infections by uropathogenic bacteria.

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Figure 1: a, Ribbon drawing of one of the 20 energy-minimized DYANA conformers of FimC used to represent the NMR structure.
Figure 2: Interdomain NOEs and interdomain contacts in FimC.
Figure 3: Logarithmic plot of backbone amide proton exchange rates (s–1) at pH 5.0 and T = 38 °C versus the amino acid sequence of FimC.
Figure 4: a–c, Stereoviews of superpositions for minimal r.m.s.d. of the backbone atoms N, Cα and C′ in the ß-strands of a representative energy-minimized DYANA conformer of FimC (blue) with the crystal structure of PapD (red and yellow).

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Acknowledgements

We thank V. Eggli for assistance with the preparation of FimC and S. Knight for providing us with coordinates of PapD and a PapD–peptide complex. Financial support was obtained from the Schweizerischer Nationalfonds to K.W. and R.G., and from an EMBO fellowship to M.P.

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  1. Maurizio Pellecchia

    Present address: Biophysics Research Division, The University of Michigan, 930 North University Avenue, Michigan, 48109, USA

Authors and Affiliations

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

    Maurizio Pellecchia, Peter Güntert, Rudi Glockshuber & Kurt Wüthrich

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

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Pellecchia, M., Güntert, P., Glockshuber, R. et al. NMR solution structure of the periplasmic chaperone FimC . Nat Struct Mol Biol 5, 885–890 (1998). https://doi.org/10.1038/2325

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