ArticleBiochemistry2012
Solution structure of a complex of the histidine autokinase CheA with its substrate CheY.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Dynamic domain interactions encode possible CheA autophosphorylation mechanisms revealed by coarse-grained simulations.Biophysical journal · 2026Article
- Dynamic domain interactions encode possible CheA autophosphorylation mechanisms revealed by coarse-grained simulations.bioRxiv : the preprint server for biology · 2025Article
- Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Diethylpyrocarbonate-Based Covalent Labeling Mass Spectrometry of Protein Interactions in a Membrane Complex System.Journal of the American Society for Mass Spectrometry · 2023Article
- Article
- Alternative Architecture of theBiomolecules · 2021Article
- ATP Binding as a Key Target for Control of the Chemotaxis Kinase.Journal of bacteriology · 2020Article
- Repurposing a chemosensory macromolecular machine.Nature communications · 2020Article
- Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations.Communications biology · 2020Article
- Regulation of the chemotaxis histidine kinase CheA: A structural perspective.Biochimica et biophysica acta. Biomembranes · 2020Review
- Site-Specific Incorporation of a CuThe journal of physical chemistry. B · 2018Article
- Article
- Spatially Heterogeneous Surface Water Diffusivity around Structured Protein Surfaces at Equilibrium.Journal of the American Chemical Society · 2017Article
- Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.Scientific reports · 2017Article
- Involvement of Two-Component Signaling on Bacterial Motility and Biofilm Development.Journal of bacteriology · 2017Review
- New Architecture for Reagentless, Protein-Based Electrochemical Biosensors.Journal of the American Chemical Society · 2017Article
- Signaling complexes control the chemotaxis kinase by altering its apparent rate constant of autophosphorylation.Protein science : a publication of the Protein Society · 2017Article
- Evolutionary Genomics Suggests That CheV Is an Additional Adaptor for Accommodating Specific Chemoreceptors within the Chemotaxis Signaling Complex.PLoS computational biology · 2016Article
- Conformational Transitions that Enable Histidine Kinase Autophosphorylation and Receptor Array Integration.Journal of molecular biology · 2015Article
- Article
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Authors and funding
4 authors.
Funding
Abstract
In the bacterial chemotaxis two-component signaling system, the histidine-containing phosphotransfer domain (the "P1" domain) of CheA receives a phosphoryl group from the catalytic domain (P4) of CheA and transfers it to the cognate response regulator (RR) CheY, which is docked by the P2 domain of CheA. Phosphorylated CheY then diffuses into the cytoplasm and interacts with the FliM moiety of the flagellar motors, thereby modulating the direction of flagellar rotation. Structures of various histidine phosphotransfer domains (HPt) complexed with their cognate RR domains have been reported. Unlike the Escherichia coli chemotaxis system, however, these systems lack the additional domains dedicated to binding to the response regulators, and the interaction of an HPt domain with an RR domain in the presence of such a domain has not been examined on a structural basis. In this study, we used modern nuclear magnetic resonance techniques to construct a model for the interaction of the E. coli CheA P1 domain (HPt) and CheY (RR) in the presence of the CheY-binding domain, P2. Our results indicate that the presence of P2 may lead to a slightly different relative orientation of the HPt and RR domains versus those seen in such complex structures previously reported.
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