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

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

C Tomomori  1 , 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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Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ

C Tomomori et al. Nat Struct Biol. 1999 Aug.

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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