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The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 Å resolution

Nature Structural Biology volume 8, pages 710–714 (2001)Cite this article

Abstract

MarR is a regulator of multiple antibiotic resistance in Escherichia coli. It is the prototypical member of the MarR family of regulatory proteins found in bacteria and archaea that play important roles in the development of antibiotic resistance, a global health problem. Here we describe the crystal structure of the MarR protein, determined at a resolution of 2.3 Å. This is the first reported crystal structure of a member of this newly-described protein family. The structure shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.

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Figure 1: The structure of MarR.
Figure 2: Regions involved in protein–protein interactions.

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Acknowledgements

This research was supported by a grant from Paratek Pharmaceuticals, Inc. and an NIH grant to S.B.L.

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Authors and Affiliations

  1. Center for Adaptation Genetics and Drug Resistance, Tufts University School of Medicine, Boston, 02111, Massachusetts, USA

    Michael N. Alekshun & Stuart B. Levy

  2. Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, 02111, Massachusetts, USA

    Michael N. Alekshun & Stuart B. Levy

  3. Paratek Pharmaceuticals Inc., Boston, 02111, Massachusetts, USA

    Michael N. Alekshun & Stuart B. Levy

  4. Department of Medicine, Tufts University School of Medicine, Boston, 02111, Massachusetts, USA

    Stuart B. Levy

  5. Department of Physiology and Biophysics, Boston University School of Medicine, Boston, 02118, Massachusetts, USA

    Tanya R. Mealy, Barbara A. Seaton & James F. Head

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  1. Michael N. Alekshun
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  2. Stuart B. Levy
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  4. Barbara A. Seaton
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  5. James F. Head
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Correspondence to James F. Head.

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Alekshun, M., Levy, S., Mealy, T. et al. The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 Å resolution. Nat Struct Mol Biol 8, 710–714 (2001). https://doi.org/10.1038/90429

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