ArticleStructure (London, England : 1993)2012
Segmental motions, not a two-state concerted switch, underlie allostery in CheY.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 58 citations in OpenAlex.
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- Remote on-off switching of protein activity by intrinsically disordered region.Nature structural & molecular biology · 2025Article
- Identifying and controlling inactive and active conformations of a serine protease.Science advances · 2025Article
- Dynamic sampling of a surveillance state enables DNA proofreading by Cas9.Cell chemical biology · 2025Article
- Regulating IL-2 Immune Signaling Function Via A Core Allosteric Structural Network.Journal of molecular biology · 2025Article
- The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding.Nature communications · 2024Article
- Role of Position K+4 in the Phosphorylation and Dephosphorylation Reaction Kinetics of the CheY Response Regulator.Biochemistry · 2021Article
- The switching mechanism of the bacterial rotary motor combines tight regulation with inherent flexibility.The EMBO journal · 2021Article
- Conformational Dynamics of Deubiquitinase A and Functional Implications.Biochemistry · 2021Article
- Modulating Enzyme FunctionFrontiers in molecular biosciences · 2021Article
- Allosteric Priming of E. coli CheY by the Flagellar Motor Protein FliM.Biophysical journal · 2020Article
- Mapping allosteric communications within individual proteins.Nature communications · 2020Article
- Modulation of Response Regulator CheY Reaction Kinetics by Two Variable Residues That Affect Conformation.Journal of bacteriology · 2020Article
- Conformational Dynamics and Cooperativity Drive the Specificity of a Protein-Ligand Interaction.Biophysical journal · 2019Article
- Biliverdin Reductase B Dynamics Are Coupled to Coenzyme Binding.Journal of molecular biology · 2018Article
- Magnesium Activates Microsecond Dynamics to Regulate Integrin-Collagen Recognition.Structure (London, England : 1993) · 2018Article
- Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase fromThe Journal of biological chemistry · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The switch between an inactive and active conformation is an important transition for signaling proteins, yet the mechanisms underlying such switches are not clearly understood. Escherichia coli CheY, a response regulator protein from the two-component signal transduction system that regulates bacterial chemotaxis, is an ideal protein for the study of allosteric mechanisms. By using 15N CPMG relaxation dispersion experiments, we monitored the inherent dynamic switching of unphosphorylated CheY. We show that CheY does not undergo a two-state concerted switch between the inactive and active conformations. Interestingly, partial saturation of Mg2+ enhances the intrinsic allosteric motions. Taken together with chemical shift perturbations, these data indicate that the μs-ms timescale motions underlying CheY allostery are segmental in nature. We propose an expanded allosteric network of residues, including W58, that undergo asynchronous, local switching between inactive and active-like conformations as the primary basis for the allosteric mechanism.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.