Reconstruction of the chemotaxis receptor–kinase assembly

@article{Park2006ReconstructionOT,
  title={Reconstruction of the chemotaxis receptor–kinase assembly},
  author={Sang-Youn Park and Peter P. Borbat and Gabriela Gonzalez-Bonet and Jaya Bhatnagar and Abiola M. Pollard and Jack H. Freed and Alexandrine M. Bilwes and Brian R. Crane},
  journal={Nature Structural \&Molecular Biology},
  year={2006},
  volume={13},
  pages={400-407}
}
In bacterial chemotaxis, an assembly of transmembrane receptors, the CheA histidine kinase and the adaptor protein CheW processes environmental stimuli to regulate motility. The structure of a Thermotoga maritima receptor cytoplasmic domain defines CheA interaction regions and metal ion–coordinating charge centers that undergo chemical modification to tune receptor response. Dimeric CheA–CheW, defined by crystallography and pulsed ESR, positions two CheWs to form a cleft that is lined with… 

Self-assembly of receptor/signaling complexes in bacterial chemotaxis

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Bacterial chemoreceptor arrays are hexagonally packed trimers of receptor dimers networked by rings of kinase and coupling proteins

This work has combined X-ray crystallography of purified proteins with electron cryotomography of native arrays inside cells to reveal the arrangement of the component transmembrane receptors, histidine kinases (CheA) and CheW coupling proteins.

Regulatory Role of an Interdomain Linker in the Bacterial Chemotaxis Histidine Kinase CheA

It is demonstrated that the interdomain linker is an active module that has the ability to impose regulatory effects on CheA activity and suggests that chemoreceptors may manipulate the conformation of the P4-P5 linker to achieve CheA regulation in the platform of the signaling complex.

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