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The crystal structure of Dps, a ferritin homolog that binds and protects DNA

Nature Structural Biology volume 5, pages 294–303 (1998)Cite this article

Abstract

The crystal structure of Dps, a DNA-binding protein from starved E. coli that protects DMA from oxidative damage, has been solved at 1.6 Å resolution. The Dps monomer has essentially the same fold as ferritin, which forms a 24-mer with 432 symmetry, a hollow core and pores at the three-fold axes. Dps forms a dodecamer with 23 (tetrahedral) point group symmetry which also has a hollow core and pores at the three-folds. The structure suggests a novel DNA-binding motif and a mechanism for DNA protection based on the sequestration of Fe ions.

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Authors and Affiliations

  1. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, 02115, USA

    R.A. Grant, D.J. Filman & J.M. Hogle

  2. Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts, 02115, USA

    S.E. Finkel & R. Kolter

  3. Committee on Higher Degrees in Biophysics, Harvard University, 240 Longwood Avenue, Boston, Massachusetts, 02115, USA

    J.M. Hogle

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  1. R.A. Grant
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  4. R. Kolter
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  5. J.M. Hogle
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Grant, R., Filman, D., Finkel, S. et al. The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat Struct Mol Biol 5, 294–303 (1998). https://doi.org/10.1038/nsb0498-294

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