ArticleJournal of molecular biology2020
Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I.
Article in Journal of molecular biology, 2020. 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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22 citing papers in PubMed.
- Application of Enzyme Engineering and Synthetic Biology for Modulated Transformation of Fructooligosaccharides (FOSs) to Elucidate the Catalytic Mechanism of Fructofuranosidases.Foods (Basel, Switzerland) · 2026Article
- Beyond structures: solution NMR as the quantitative engine of integrated structural biology.Frontiers in molecular biosciences · 2026Review
- Response surface optimization for cellulase production from Enterococcus faecium and Stutzerimonas stutzeri isolated from Gossypium arboretum and Solanum melongena soil.Scientific reports · 2025Article
- Maltodextrin transport in the extremely thermophilic, lignocellulose degrading bacteriumJournal of bacteriology · 2025Article
- Illuminating Protein Allostery by Chemically Accurate Contact Response Analysis (ChACRA).Journal of chemical theory and computation · 2024Article
- 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
- Selective enhanced cytotoxicity of amino acid deprivation for cancer therapy using thermozyme functionalized nanocatalyst.Journal of nanobiotechnology · 2024Article
- Sugar transport in thermophiles: Bridging lignocellulose deconstruction and bioconversion.Journal of industrial microbiology & biotechnology · 2024Review
- Hydrogen spillover and substrate-support hydrogen bonding mediate hydrogenation of phenol catalyzed by palladium on reducible metal oxides.Chemical science · 2023Article
- 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
- Temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymes.Frontiers in molecular biosciences · 2023Review
- 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
- Solution structure ensemble of human obesity-associated protein FTO reveals druggable surface pockets at the interface between the N- and C-terminal domain.The Journal of biological chemistry · 2022Article
- Structural and dynamic insights into the HNH nuclease of divergent Cas9 species.Journal of structural biology · 2022Article
- 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
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6 authors.
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Abstract
Conformational disorder is emerging as an important feature of biopolymers, regulating a vast array of cellular functions, including signaling, phase separation, and enzyme catalysis. Here we combine NMR, crystallography, computer simulations, protein engineering, and functional assays to investigate the role played by conformational heterogeneity in determining the activity of the C-terminal domain of bacterial Enzyme I (EIC). In particular, we design chimeric proteins by hybridizing EIC from thermophilic and mesophilic organisms, and we characterize the resulting constructs for structure, dynamics, and biological function. We show that EIC exists as a mixture of active and inactive conformations and that functional regulation is achieved by tuning the thermodynamic balance between active and inactive states. Interestingly, we also present a hybrid thermophilic/mesophilic enzyme that is thermostable and more active than the wild-type thermophilic enzyme, suggesting that hybridizing thermophilic and mesophilic proteins is a valid strategy to engineer thermostable enzymes with significant low-temperature activity.
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