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Structure of the arginine repressor from Bacillus stearothermophilus

Nature Structural Biology volume 6, pages 427–432 (1999)Cite this article

Abstract

The arginine repressor (ArgR) is a hexameric DNA-binding protein that plays a multifunctional role in the bacterial cell. Here, we present the 2.5 Å structure of apo-ArgR from Bacillus stearothermophilus and the 2.2 Å structure of the hexameric ArgR oligomerization domain with bound arginine. This first view of intact ArgR reveals an approximately 32-symmetric hexamer of identical subunits, with six DNA-binding domains surrounding a central oligomeric core. The difference in quaternary organization of subunits in the arginine-bound and apo forms provides a possible explanation for poor operator binding by apo-ArgR and for high affinity binding in the presence of arginine.

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Figure 1: a, Aligned sequences of the arginine repressors from E. coli5, H. influenzae9, M. tuberculosis 10, S. clavuligerus11, B. subtilis 6, and B. stearothermophilus8 (the first 11 residues of M. tuberculosis ArgR are not shown).
Figure 2: a, Ribbon drawing of the ArgRBst-C hexamer, viewed along the local threefold symmetry axis.
Figure 3: a, Ribbon drawing of apo-ArgRBst, viewed down the pseudo-three-fold axis of the hexamer.
Figure 4: a, Model of the apo-ArgRBst–DNA interaction.

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Acknowledgements

We thank the staff of the CHESS F1 beamline for synchrotron support, F. Guo and M. Gopaul for assistance with data collection, and X. Li for help in crystallization. We also acknowledge helpful comments and discussions from M. Lemmon, H. Lu, H. Nelson, M. Lewis, and W.K. Maas. Supported by a grant from the National Institutes of Health to G.V.

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Authors and Affiliations

  1. Department of Biotechnology & Biophysics and Johson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, 19104, Pennsylvania, USA

    Jianping Ni & Gregory D. Van Duyne

  2. Laboratoire de Biotechnologie, UPRES Biocatalyse, Faculté des Sciences et des Techniques, Université de Nantes, Nantes , F-44072, France

    Vehary Sakanyan

  3. Research Institute of the CERIA-COOVI, Microbiology, Free University of Brussels & Flanders Interuniversity Institute fro Biotechnology , Brussels, B-1070, Belgium

    Daniel Charlier & Nicolas Glansdorff

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  1. Jianping Ni
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  2. Vehary Sakanyan
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  5. Gregory D. Van Duyne
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Correspondence to Gregory D. Van Duyne.

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Ni, J., Sakanyan, V., Charlier, D. et al. Structure of the arginine repressor from Bacillus stearothermophilus . Nat Struct Mol Biol 6, 427–432 (1999). https://doi.org/10.1038/8229

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