ArticleScientific reports2017
The relationship between folding and activity in UreG, an intrinsically disordered enzyme.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Structural and Functional Characterization of LIMCH1 and Its Agmatinase-like Region: A Case of Catalysis in a Highly Disordered Protein.Biomolecules · 2025Article
- Hidden protein disorder: Deciphering the structural organisation and dynamics of a non-canonical CP12 from the diatom Thalassiosira pseudonana.The FEBS journal · 2025Article
- A suicidal and extensively disordered luciferase with a bright luminescence.Protein science : a publication of the Protein Society · 2024Article
- Article
- Guidelines for the Simulations of Nitroxide X-Band cw EPR Spectra from Site-Directed Spin Labeling Experiments Using SMolecules (Basel, Switzerland) · 2023Article
- Mapping the Constrained Coding Regions in the Human Genome to Their Corresponding Proteins.Journal of molecular biology · 2023Article
- The Disordered Amino Terminus of the Circadian Enzyme Nocturnin Modulates Its NADP(H) Phosphatase Activity by Changing Protein Dynamics.Biochemistry · 2022Article
- Intrinsically Disordered Proteins: Critical Components of the Wetware.Chemical reviews · 2022Review
- Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1.Frontiers 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
- Nickel and GTP ModulateBiomolecules · 2020Article
- The Order-Disorder Continuum: Linking Predictions of Protein Structure and Disorder through Molecular Simulation.Scientific reports · 2020Review
- Genomics of Urea Transport and Catabolism in Cyanobacteria: Biotechnological Implications.Frontiers in microbiology · 2019Review
- Intrinsically Disordered Proteins and the Janus Challenge.Biomolecules · 2018Article
- Active Site Breathing of Human Alkbh5 Revealed by Solution NMR and Accelerated Molecular Dynamics.Biophysical journal · 2018Article
- Ureases: Historical aspects, catalytic, and non-catalytic properties - A review.Journal of advanced research · 2018Review
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A growing body of literature on intrinsically disordered proteins (IDPs) led scientists to rethink the structure-function paradigm of protein folding. Enzymes are often considered an exception to the rule of intrinsic disorder (ID), believed to require a unique structure for catalysis. However, recent studies revealed the presence of disorder in several functional native enzymes. In the present work, we address the importance of dynamics for catalysis, by investigating the relationship between folding and activity in Sporosarcina pasteurii UreG (SpUreG), a P-loop GTPase and the first discovered native ID enzyme, involved in the maturation of the nickel-containing urease. The effect of denaturants and osmolytes on protein structure and activity was analyzed using circular dichroism (CD), Site-Directed Spin Labeling (SDSL) coupled to EPR spectroscopy, and enzymatic assays. Our data show that SpUreG needs a "flexibility window" to be catalytically competent, with both too low and too high mobility being detrimental for its activity.
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