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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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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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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DOI: https://doi.org/10.1038/8229
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