Structure of CheA, a Signal-Transducing Histidine Kinase

@article{Bilwes1999StructureOC,
  title={Structure of CheA, a Signal-Transducing Histidine Kinase},
  author={Alexandrine M. Bilwes and Lisa A. Alex and Brian R. Crane and Melvin I. Simon},
  journal={Cell},
  year={1999},
  volume={96},
  pages={131-141}
}

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References

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Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
TLDR
The crystal structure of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA, suggests that molecular recognition, in this low affinity complex, may also contribute to the mechanism of CheY activation.
Two-domain reconstitution of a functional protein histidine kinase.
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    Proceedings of the National Academy of Sciences of the United States of America
  • 1998
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)].
Expression of CheA fragments which define domains encoding kinase, phosphotransfer, and CheY binding activities.
TLDR
Genes encoding three polypeptide fragments of CheA were constructed and expressed in order to better define the functional organization of the wild-type protein and allowed the identification of regions of the protein responsible for CheY binding, phosphotransfer, and kinase activity.
Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
Bacterial chemotaxis involves autophosphorylation of a histidine kinase and transfer of the phosphoryl group to response regulators to control flagellar rotation and receptor adaptation. The
Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway.
TLDR
The crystal structure at 2.0-A resolution of the complex of the Escherichia coli chemotaxis response regulator CheY and the phosphoacceptor-binding domain (P2) of the kinase CheA is presented, suggesting that the plasticity of CheY is an essential feature of response regulator function.
Intermolecular complementation of the kinase activity of CheA
TLDR
Results indicate that the dimeric form of CheA plays an integral role in signal transduction in bacterial chemotaxis, and is required for regulation in response to environmental signals transmitted through a transducer and CheW.
The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW
TLDR
Three functional domains of the CheA protein are delineated - the amino-terminal portion of CheA was previously shown to contain the site of autophosphorylation and to be able to transfer the phosphoryl group to CheB and CheY.
NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics.
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.
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