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

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, Masatsune Kainosho, Masayori Inouye and Mitsuhiko Ikura ()
Additional contact information
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.
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

Nature, 1998, vol. 396, issue 6706, 88-92

Abstract: 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.

Date: 1998
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DOI: 10.1038/23968

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