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Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli

Nature Structural Biology volume 7, pages 196–199 (2000)Cite this article

Abstract

DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is thought to function as a disulfide bond isomerase during oxidative protein folding in the periplasm. DsbC is a 2 × 23 kDa homodimer and has both protein disulfide isomerase and chaperone activity. We report the 1.9 Å resolution crystal structure of oxidized DsbC where both Cys-X-X-Cys active sites form disulfide bonds. The molecule consists of separate thioredoxin-like domains joined via hinged linker helices to an N-terminal dimerization domain. The hinges allow relative movement of the active sites, and a broad uncharged cleft between them may be involved in peptide binding and DsbC foldase activities.

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Figure 1: Three-dimensional structure of DsbC.
Figure 2: The hydrophobic cleft.
Figure 3: Comparison of DsbC homologs and DsbG.
Figure 4: The DsbC active site.

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Acknowledgements

We thank former EMBL colleagues for their support: T. Creighton for suggesting the project, A. Zapun and N. Darby for materials and advice, M. Neu for help with purification and crystallization, and A. Thompson for MAD beamline support. P.W.H. is supported by the Daimler-Benz Stiftung and Boehringer Ingelheim Fonds. We also acknowledge support from the Health Research Council of New Zealand and the Wellcome Trust. E.N.B. is a Howard Hughes International Research Scholar.

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Author notes

  1. Andrew A. McCarthy, Peter W. Haebel and Vladimir Rybin: These authors contributed equally to this work.

Authors and Affiliations

  1. School of Biological Sciences, Auckland University, Private Bag, Auckland, 92019, New Zealand

    Andrew A. McCarthy, Peter W. Haebel, Edward N. Baker & Peter Metcalf

  2. Danisco (Cultor), Technology Center, Kantvik, FIN-02460, Finlandtill

    Anneli Törrönen

  3. EMBL Heidelberg, Meyerhofstrasse 1, Postfach 10.2209, Heidelberg, D-69012, Germany

    Vladimir Rybin

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  1. Andrew A. McCarthy
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Correspondence to Peter Metcalf.

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McCarthy, A., Haebel, P., Törrönen, A. et al. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nat Struct Mol Biol 7, 196–199 (2000). https://doi.org/10.1038/73295

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