ArticleNature communications2015
Structural basis for catalytically restrictive dynamics of a high-energy enzyme state.
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 25 papers.
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Who cites it
25 citing papers in PubMed.
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- Hydrophobic interactions determine the optimum temperature of a housekeeping enzyme.The Journal of biological chemistry · 2026Article
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- AlphaFold-guided molecular replacement for solving challenging crystal structures.Acta crystallographica. Section D, Structural biology · 2025Article
- Allostery can convert binding free energies into concerted domain motions in enzymes.Nature communications · 2024Article
- Enzyme activation by urea reveals the interplay between conformational dynamics and substrate binding: a single-molecule FRET study.bioRxiv : the preprint server for biology · 2024Article
- Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development.ACS omega · 2024Review
- Conformational dynamics of adenylate kinase in crystals.Structural dynamics (Melville, N.Y.) · 2024Article
- Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Insights into the evolution of enzymatic specificity and catalysis: From Asgard archaea to human adenylate kinases.Science advances · 2022Article
- Role of Repeated Conformational Transitions in Substrate Binding of Adenylate Kinase.The journal of physical chemistry. B · 2022Article
- Frustration and the Kinetic Repartitioning Mechanism of Substrate Inhibition in Enzyme Catalysis.The journal of physical chemistry. B · 2022Article
- Tracking the ATP-binding response in adenylate kinase in real time.Science advances · 2021Article
- Structural and functional consequences of NEDD8 phosphorylation.Nature communications · 2021Article
- Structural Basis for GTP versus ATP Selectivity in the NMP Kinase AK3.Biochemistry · 2020Article
- Article
- Conformational and functional characterization of artificially conjugated non-canonical ubiquitin dimers.Scientific reports · 2019Article
- Liquid Metastable Precursors of Ibuprofen as Aqueous Nucleation Intermediates.Angewandte Chemie (International ed. in English) · 2019Article
- Development of Software for the In-Depth Analysis of Protein Dynamics as Determined by MALDI Mass Spectrometry-Based Hydrogen/Deuterium Exchange.Mass spectrometry (Tokyo, Japan) · 2019Article
- A Luminal Loop of Wilson Disease Protein Binds Copper and Is Required for Protein Activity.Biophysical journal · 2018Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An emerging paradigm in enzymology is that transient high-energy structural states play crucial roles in enzymatic reaction cycles. Generally, these high-energy or 'invisible' states cannot be studied directly at atomic resolution using existing structural and spectroscopic techniques owing to their low populations or short residence times. Here we report the direct NMR-based detection of the molecular topology and conformational dynamics of a catalytically indispensable high-energy state of an adenylate kinase variant. On the basis of matching energy barriers for conformational dynamics and catalytic turnover, it was found that the enzyme's catalytic activity is governed by its dynamic interconversion between the high-energy state and a ground state structure that was determined by X-ray crystallography. Our results show that it is possible to rationally tune enzymes' conformational dynamics and hence their catalytic power--a key aspect in rational design of enzymes catalysing novel reactions.
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