Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ

C. Tomomori, T. Tanaka, R. Dutta, H. Park, S. K. Saha, Y. Zhu, R. Ishima, D. Liu, K. I. Tong, H. Kurokawa, H. Qian, M. Inouye, M. Ikura

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195 Scopus citations

Abstract

Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions. Here we present the NMR-derived structure of the homodimeric core domain (residues 223-289) of EnvZ that includes His 243, the site of autophosphorylation and phosphate transfer reactions. The structure comprises a four-helix bundle formed by two identical helix-turn-helix subunits, revealing the molecular assembly of two active sites within the dimeric kinase.

Original languageEnglish (US)
Pages (from-to)729-734
Number of pages6
JournalNature structural biology
Volume6
Issue number8
DOIs
StatePublished - Aug 10 1999
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Genetics
  • Structural Biology
  • Biochemistry

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    Tomomori, C., Tanaka, T., Dutta, R., Park, H., Saha, S. K., Zhu, Y., Ishima, R., Liu, D., Tong, K. I., Kurokawa, H., Qian, H., Inouye, M., & Ikura, M. (1999). Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. Nature structural biology, 6(8), 729-734. https://doi.org/10.1038/11495