Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ
- PMID: 10426948
- DOI: 10.1038/11495
Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ
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.
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