Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. |
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| Authors: | C Tomomori 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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| Institution: | Center for Tsukuba Advanced Research Alliance and Institute of Applied Biochemistry, University of Tsukuba, Tsukuba, Ibaraki 305-8577, Japan. |
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| 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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