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Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY

Nature Structural Biology volume 5, pages 25–29 (1998)Cite this article

Abstract

Bacterial adaptation to the environment is accomplished through the coordinated activation of specific sensory receptors and signal processing proteins. Among the best characterized of these pathways are those which employ the two-component paradigm. In these systems, signal transmission is mediated by Mg2+-dependent phospho-relay reactions between histidine auto-kinases and phosphoaccepting receiver domains in response-regulator proteins. Although this mechanism of activation is common to all response-regulators, detrimental cross-talk between different two-component pathways within the same cell is minimized through the use of specific recognition domains. Here, we report the crystal structure, at 2.95 Å resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA. The structure suggests that molecular recognition, in this low affinity complex (KD = 2 μM), may also contribute to the mechanism of CheY activation.

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Author notes

  1. Natalie Chinardet: These authors made equal contribution to this work.

Authors and Affiliations

  1. Institut de Pharmacologie et de Biologie Structural CNRS, UPR9062, 205 route de Narbonne, 31077, Toulouse, France

    Martin Welch, Lionel Mourey, Catherine Birck & Jean-Pierre Samama

Authors
  1. Martin Welch
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  2. Natalie Chinardet
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  3. Lionel Mourey
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  4. Catherine Birck
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  5. Jean-Pierre Samama
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Correspondence to Jean-Pierre Samama.

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Welch, M., Chinardet, N., Mourey, L. et al. Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nat Struct Mol Biol 5, 25–29 (1998). https://doi.org/10.1038/nsb0198-25

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