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NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ

Author

Listed:
  • Toshiyuki Tanaka

    (Center for Tsukuba Advanced Research Alliance and Institute of Applied Biochemistry, University of Tsukuba)

  • Soumitra K. Saha

    (Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey)

  • Chieri Tomomori

    (Center for Tsukuba Advanced Research Alliance and Institute of Applied Biochemistry, University of Tsukuba)

  • Rieko Ishima

    (University of Toronto)

  • Dingjiang Liu

    (University of Toronto)

  • Kit I. Tong

    (University of Toronto)

  • Heiyoung Park

    (Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey)

  • Rinku Dutta

    (Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey)

  • Ling Qin

    (Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey)

  • Mark B. Swindells

    (Helix Research Institute Inc.
    Inpharmatica Ltd)

  • Toshimasa Yamazaki

    (National Institute of Agrobiological Resources)

  • Akira M. Ono

    (Tokyo Metropolitan University)

  • Masatsune Kainosho

    (Tokyo Metropolitan University)

  • Masayori Inouye

    (Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey)

  • Mitsuhiko Ikura

    (University of Toronto)

Abstract

Bacteria live in capricious environments, in which they must continuously sense external conditions in order to adjust their shape, motility and physiology1. The histidine–aspartate phosphorelay signal-transduction system (also known as the two-component system) is important in cellular adaptation to environmental changes in both prokaryotes and lower eukaryotes2,3. In this system, protein histidine kinases function as sensors and signal transducers. The Escherichia coli osmosensor, EnvZ, is a transmembrane protein with histidine kinase activity in its cytoplasmic region2. The cytoplasmic region contains two functional domains4: domain A (residues 223–289) contains the conserved histidine residue (H243), a site of autophosphorylation as well as transphosphorylation to the conserved D55 residue of response regulator OmpR, whereas domain B (residues 290–450) encloses several highly conserved regions (G1, G2, F and N boxes) and is able to phosphorylate H243. Here we present the solution structure of domain B, the catalytic core of EnvZ. This core has a novel protein kinase structure, distinct from the serine/threonine/tyrosine kinase fold, with unanticipated similarities to both heat-shock protein 90 and DNA gyrase B.

Suggested Citation

  • Toshiyuki Tanaka & Soumitra K. Saha & Chieri Tomomori & Rieko Ishima & Dingjiang Liu & Kit I. Tong & Heiyoung Park & Rinku Dutta & Ling Qin & Mark B. Swindells & Toshimasa Yamazaki & Akira M. Ono & Ma, 1998. "NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ," Nature, Nature, vol. 396(6706), pages 88-92, November.
    • Handle: RePEc:nat:nature:v:396:y:1998:i:6706:d:10.1038_23968
    DOI: 10.1038/23968
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