Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ.
Article Details
- CitationCopy to clipboard
Tomomori C, Tanaka T, Dutta R, Park H, Saha SK, Zhu Y, Ishima R, Liu D, Tong KI, Kurokawa H, Qian H, Inouye M, Ikura M
Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ.
Nat Struct Biol. 1999 Aug;6(8):729-34.
- PubMed ID
- 10426948 [ View in PubMed]
- 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.