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Crystal structure of an activated response regulator bound to its target

Nature Structural Biology volume 8, pages 52–56 (2001)Cite this article

Abstract

The chemotactic regulator CheY controls the direction of flagellar rotation in Escherichia coli. We have determined the crystal structure of BeF3−-activated CheY from E. coli in complex with an N-terminal peptide derived from its target, FliM. The structure reveals that the first seven residues of the peptide pack against the β4-H4 loop and helix H4 of CheY in an extended conformation, whereas residues 8–15 form two turns of helix and pack against the H4-β5-H5 face. The peptide binds the only region of CheY that undergoes noticeable conformational change upon activation and would most likely be sandwiched between activated CheY and the remainder of FliM to reverse the direction of flagellar rotation.

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Figure 1: Sequence alignment and ribbon diagram of the BeF3−–CheY–N16-FliM complex.
Figure 2: Stereo view of the active site of CheY showing the Fo − Fc electron density for the BeF3− moiety contoured at 5.5 σ.
Figure 3: GRASP33 electrostatic surface representations of:
Figure 4: Stereo view of the CheY–N16-FliM interface.

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Acknowledgements

We thank H. Bellamy for performing the X-ray fluorescence scan and help in designing the MAD experiment at SSRL. We thank T. Earnest (ALS) and D. Shin (Physical Biosciences Division, LBL) for helpful advice and encouragement. This work was supported by the Office of Energy Research, Office of Health and Environmental Research, Health Effects Research Division of the U.S. Department of Energy (D.E.W.) and National Institutes of Health (S.K.) and through instrumentation grants from the U.S. Department of Energy and the National Science Foundation (D.E.W.). This work was done (partially) at SSRL which is operated by the Department of Energy, Office of Basic Energy Sciences. The SSRL Biotechnology Program is supported by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and by the Department of Energy, Office of Biological and Environmental Research.

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Authors and Affiliations

  1. Graduate Group in Biophysics, University of California, Berkeley, 94720, California, USA

    Seok-Yong Lee & David E. Wemmer

  2. Physical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, 94720, California, USA

    Seok-Yong Lee, Ho S. Cho, Jeffrey G. Pelton, Robert K. Henderson, Li-shar Huang, Edward A. Berry & David E. Wemmer

  3. Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, Berkeley, 94720, California, USA

    Ho S. Cho, Dalai Yan & Sydney Kustu

  4. Howard Hughes Medical Institute and Department of Molecular and Cell Biology, 381 Koshland Hall

    David S. King

  5. University of California, Berkeley, 94720, California, USA

    David S. King

  6. Department of Chemistry, University of California, Berkeley, 94720, California, USA

    David E. Wemmer

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  1. Seok-Yong Lee
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Correspondence to David E. Wemmer.

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Lee, SY., Cho, H., Pelton, J. et al. Crystal structure of an activated response regulator bound to its target. Nat Struct Mol Biol 8, 52–56 (2001). https://doi.org/10.1038/83053

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