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

Nature Structural & Molecular Biology volume 6, pages 729–734 (1999) Cite this article

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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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Figure 1: Three-dimensional structure of EnvZ domain A.
Figure 2: Hydrophobic core and sequence alignment of EnvZ domain A.
Figure 3: Interaction between EnvZ and OmpR.
Figure 4: Summary of mutations in EnvZ domain A.

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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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Author notes

  1. Rieko Ishima

    Present address: Molecular Structural Biology Unit, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland, 20892, USA

  2. Dingjiang Liu

    Present address: Schering-Plough Research Institute, Kenilworth, New Jersey, 07033-0539, USA

Authors and Affiliations

  1. Center for Tsukuba Advanced Research Alliance and Institute of Applied Biochemistry, University of Tsukuba, Tsukuba, 305-8577, Ibaraki, Japan

    Chieri Tomomori & Toshiyuki Tanaka

  2. Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, 08854, New Jersey, USA

    Rinku Dutta, Heiyoung Park, Soumitra K. Saha, Yan Zhu & Masayori Inouye

  3. Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, M5G 2M9, Ontario, Canada

    Rieko Ishima, Dingjiang Liu, Kit I. Tong, Hirofumi Kurokawa, Hong Qian & Mitsuhiko Ikura

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  1. Chieri Tomomori
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Correspondence to Masayori Inouye or Mitsuhiko Ikura.

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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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