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

Nat Struct Biol. 1999 Aug;6(8):729-34. doi: 10.1038/11495.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / genetics
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins*
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Multienzyme Complexes*
  • Mutagenesis, Site-Directed
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Solutions


  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • Multienzyme Complexes
  • Solutions
  • envZ protein, E coli

Associated data

  • PDB/1JOY