ArticleNature communications2015
Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Integrating NMR and contact-response analysis reveals the allosteric network driving domain closure in Enzyme I.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Beyond structures: solution NMR as the quantitative engine of integrated structural biology.Frontiers in molecular biosciences · 2026Review
- An α-ketoglutarate conformational switch controls iron accessibility, activation, and substrate selection of the human FTO protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Elucidation of the Mechanisms of Inter-domain Coupling in the Monomeric State of Enzyme I by High-pressure NMR.Journal of molecular biology · 2024Article
- Solution Structure Ensembles of the Open and Closed Forms of the ∼130 kDa Enzyme I via AlphaFold Modeling, Coarse Grained Simulations, and NMR.Journal of the American Chemical Society · 2023Article
- Protein Conformational Dynamics Underlie Selective Recognition of Thermophilic over Mesophilic Enzyme I by a Substrate Analogue.Biomolecules · 2023Article
- Visualizing the transiently populated closed-state of human HSP90 ATP binding domain.Nature communications · 2022Article
- Temperature-sensitive contacts in disordered loops tune enzyme I activity.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Solution NMR methods for structural and thermodynamic investigation of nanoparticle adsorption equilibria.Nanoscale advances · 2022Review
- Article
- Structure elucidation of the elusive Enzyme I monomer reveals the molecular mechanisms linking oligomerization and enzymatic activity.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- 15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale.Journal of visualized experiments : JoVE · 2021Article
- A Single Point Mutation Controls the Rate of Interconversion Between theFrontiers in molecular biosciences · 2021Article
- Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I.Journal of molecular biology · 2020Article
- N-terminal fusion of the N-terminal domain of bacterial enzyme I facilitates recombinant expression and purification of the human RNA demethylases FTO and Alkbh5.Protein expression and purification · 2020Article
- An allosteric pocket for inhibition of bacterial Enzyme I identified by NMR-based fragment screening.Journal of structural biology: X · 2020Article
- Retinoic Acid Binding Leads to CRABP2 Rigidification and Dimerization.Biochemistry · 2019Article
- Active Site Breathing of Human Alkbh5 Revealed by Solution NMR and Accelerated Molecular Dynamics.Biophysical journal · 2018Article
- The oligomerization state of bacterial enzyme I (EI) determines EI's allosteric stimulation or competitive inhibition by α-ketoglutarate.The Journal of biological chemistry · 2018Article
- Dimerization facilitates the conformational transitions for bacterial phosphotransferase enzyme I autophosphorylation in an allosteric manner.FEBS open bio · 2017Article
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Authors and funding
5 authors.
Funding
Abstract
Enzyme I (EI), the first component of the bacterial phosphotransfer signal transduction system, undergoes one of the largest substrate-induced interdomain rearrangements documented to date. Here we characterize the perturbations generated by two small molecules, the natural substrate phosphoenolpyruvate and the inhibitor α-ketoglutarate, on the structure and dynamics of EI using NMR, small-angle X-ray scattering and biochemical techniques. The results indicate unambiguously that the open-to-closed conformational switch of EI is triggered by complete suppression of micro- to millisecond dynamics within the C-terminal domain of EI. Indeed, we show that a ligand-induced transition from a dynamic to a more rigid conformational state of the C-terminal domain stabilizes the interface between the N- and C-terminal domains observed in the structure of the closed state, thereby promoting the resulting conformational switch and autophosphorylation of EI. The mechanisms described here may be common to several other multidomain proteins and allosteric systems.
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