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 language | English |
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Pages (from-to) | 729-734 |
Number of pages | 6 |
Journal | Nature Structural Biology |
Volume | 6 |
Issue number | 8 |
DOIs | |
Publication status | Published - 1999 Aug 10 |
Externally published | Yes |
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics