ArticleJournal of molecular biology2013
Colocalization of fast and slow timescale dynamics in the allosteric signaling protein CheY.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed.
- The protein-water H-bond network for bacterial response regulator REC domain activation.Journal of structural biology: X · 2026Article
- Advances in uncovering the mechanisms of macromolecular conformational entropy.Nature chemical biology · 2025Review
- Article
- A hierarchy of coupling free energies underlie the thermodynamic and functional architecture of protein structures.Current research in structural biology · 2021Review
- Energy Bilocalization Effect and the Emergence of Molecular Functions in Proteins.Frontiers in molecular biosciences · 2021Article
- Mapping allosteric communications within individual proteins.Nature communications · 2020Article
- Multiple CheY Homologs Control Swimming Reversals and Transient Pauses in Azospirillum brasilense.Biophysical journal · 2019Article
- Green Rust: The Simple Organizing 'Seed' of All Life?Life (Basel, Switzerland) · 2018Review
- Why the Energy Landscape of Barnase Is Hierarchical.Frontiers in molecular biosciences · 2018Article
- Role of Terahertz (THz) Fluctuations in the Allosteric Properties of the PDZ Domains.The journal of physical chemistry. B · 2017Article
- Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase fromThe Journal of biological chemistry · 2017Article
- Effect of Phosphorylation on a Human-like Osteopontin Peptide.Biophysical journal · 2017Article
- Widespread Perturbation of Function, Structure, and Dynamics by a Conservative Single-Atom Substitution in Thymidylate Synthase.Biochemistry · 2016Article
- ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation.Nature communications · 2016Article
- Prediction of allosteric sites and mediating interactions through bond-to-bond propensities.Nature communications · 2016Article
- What Mutagenesis Can and Cannot Reveal About Allostery.Biophysical journal · 2016Review
- Dynamically Driven Protein Allostery Exhibits Disparate Responses for Fast and Slow Motions.Biophysical journal · 2015Article
- Ligand-induced folding of a two-component signaling receiver domain.Biochemistry · 2015Article
- Article
- Evidence against the "Y-T coupling" mechanism of activation in the response regulator NtrC.Journal of molecular biology · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
It is now widely recognized that dynamics are important to consider for understanding allosteric protein function. However, dynamics occur over a wide range of timescales, and how these different motions relate to one another is not well understood. Here, we report an NMR relaxation study of dynamics over multiple timescales at both backbone and side-chain sites upon an allosteric response to phosphorylation. The response regulator, Escherichia coli CheY, allosterically responds to phosphorylation with a change in dynamics on both the microsecond-to-millisecond (μs-ms) timescale and the picosecond-to-nanosecond (ps-ns) timescale. We observe an apparent decrease and redistribution of μs-ms dynamics upon phosphorylation (and accompanying Mg(2+) saturation) of CheY. Additionally, methyl groups with the largest changes in ps-ns dynamics localize to the regions of conformational change measured by μs-ms dynamics. The limited spread of changes in ps-ns dynamics suggests a distinct relationship between motions on the μs-ms and ps-ns timescales in CheY. The allosteric mechanism utilized by CheY highlights the diversity of roles dynamics play in protein function.
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Registered trials
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