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

@article{Tomomori1999SolutionSO,
  title={Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ},
  author={Chieri Tomomori and Toshiyuki Tanaka and Rinku Dutta and Heiyoung Park and Soumitra K. Saha and Yan Zhu and Rieko Ishima and Dingjiang Liu and Kit I. Tong and Hirofumi Kurokawa and H Qian and Masayori Inouye and Mitsuhiko Ikura},
  journal={Nature Structural Biology},
  year={1999},
  volume={6},
  pages={729-734}
}
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… 
A monomeric histidine kinase derived from EnvZ, an Escherichia coli osmosensor
TLDR
It is demonstrated for the first time the construction of a functional, monomeric histidine kinase by fusing in tandem two domains A and one domain B to produce a single polypeptide (A–A–B).
Structural characterization of Escherichia coli sensor histidine kinase EnvZ: the periplasmic C-terminal core domain is critical for homodimerization.
TLDR
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TLDR
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Cysteine-Scanning Analysis of the Dimerization Domain of EnvZ, an Osmosensing Histidine Kinase
TLDR
A cysteine-scanning analysis of domain A, a 67-residue central dimerization and phosphatase domain containing His-243 as the phosphorylation site, indicates that some mutations are specific either for the phosphat enzyme activity or for the kinase activity.
Mechanism of regulation of the bifunctional histidine kinase NtrB in Escherichia coli.
TLDR
NtrB is the bifunctional histidine kinase for nitrogen regulation, which either autophosphorylates and serves as the phosphodonor for its cognate response regulator, NtrC, or, it promotes the rapid dephosphorylation of NtrP-P.
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References

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NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ
TLDR
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.
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    Proceedings of the National Academy of Sciences of the United States of America
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TLDR
It is demonstrated that the cytoplasmic kinase domain of EnvZ, a transmembrane osmosensor of Escherichia coli can be further divided into two distinct functional subdomains: subdomain A [EnvZ(C)].
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TLDR
To study the structural requirements for these two states of EnvZ, mutational analysis was performed and identified a novel motif that is weakly conserved among two-component sensors.
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TLDR
The protein backbone dynamics studies show that CheA1-134 is formed into a tight and compact structure with very limited flexibilities both in helices and turns, and the NMR relaxation properties of the backbone 15N nuclei are measured using inverse detected two-dimensional NMR spectroscopy.
Function of conserved histidine-243 in phosphatase activity of EnvZ, the sensor for porin osmoregulation in Escherichia coli
TLDR
The mutated histidine-243 was mutated to several other amino acids and the phosphatase activity of mutated EnvZ was measured both in vivo and in vitro, indicating that although conserved histidine -243 is important for the phosph atase activity, a histidine,243-P intermediate is not required.
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