Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway

Megan McEvoy, Andrew Hausrath, Gannon B. Randolph, S. James Remington, Frederick W. Dahlquist

Research output: Contribution to journalArticle

81 Scopus citations


The crystal structure at 2.0-Å resolution of the complex of the Escherichia coli chemotaxis response regulator CheY and the phosphoacceptor- binding domain (P2) of the kinase CheA is presented. The binding interface involves the fourth and fifth helices and fifth β-strand of CheY and both helices of P2. Surprisingly, the two heterodimers in the asymmetric unit have two different binding modes involving the same interface, suggesting some flexibility in the binding regions. Significant conformational changes have occurred in CheY compared with previously determined unbound structures. The active site of CheY is exposed by the binding of the kinase domain, possibly to enhance phosphotransfer from CheA to CheY. The conformational changes upon complex formation as well as the observation that there are two different binding modes suggest that the plasticity of CheY is an essential feature of response regulator function.

Original languageEnglish (US)
Pages (from-to)7333-7338
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number13
Publication statusPublished - Jun 23 1998
Externally publishedYes


ASJC Scopus subject areas

  • Genetics
  • General

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