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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Acknowledgements
We thank L. Kay for providing NMR pulse sequences, D. Garrett for helpful instructions on PIPP/STAPP, M. Osawa for providing software used in structure calculation, K. Yap for calculation of interhelical angles, and S. Bagby for critical reading of the manuscript. This work was supported by grants to T.T. from JSPS, to M. Inouye from the NIH, and to M. Ikura from the Howard Hughes Medical Institute. R.I. and D.L. acknowledge HFSP postdoctoral fellowships, and C.T. a postgraduate fellowship from the Ministry of Education, Science and Culture of Japan and from the TARA, University of Tsukuba. M. Ikura is an HHMI International esearch Scholar and a Medical Research Council of Canada Scientist.
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Tomomori, C., Tanaka, T., Dutta, R. et al. Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ . Nat Struct Mol Biol 6, 729–734 (1999). https://doi.org/10.1038/11495
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DOI: https://doi.org/10.1038/11495
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