ArticleNature structural & molecular biology2011
Competing allosteric mechanisms modulate substrate binding in a dimeric enzyme.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
45 citing papers in PubMed.
- The Ensemble Basis of Allostery and Function: Insights from Models of Local Unfolding.Journal of molecular biology · 2025Review
- Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography.Nature communications · 2025Article
- Dynamic energy conversion in protein catalysis: From brownian motion to enzymatic function.Computational and structural biotechnology journal · 2025Review
- Altering Active-Site Loop Dynamics Enhances Standalone Activity of the Tryptophan Synthase Alpha Subunit.ACS catalysis · 2024Article
- Improved Catalytic Activity of Spherical Nucleic Acid Enzymes by Hybridization Chain Reaction and Its Application for Sensitive Analysis of Aflatoxin B1.Sensors (Basel, Switzerland) · 2024Article
- A three-level regulatory mechanism of the aldo-keto reductase subfamily AKR12D.Nature communications · 2024Article
- Machine learning and protein allostery.Trends in biochemical sciences · 2023Review
- Selective Monofunctionalization Enabled by Reaction-History-Dependent Communication in Catalytic Rotaxanes.Angewandte Chemie (International ed. in English) · 2020Article
- Structural analysis of a novel substrate-free form of the aminoglycoside 6'-N-acetyltransferase from Enterococcus faecium.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Nanosecond-Timescale Dynamics and Conformational Heterogeneity in Human GCK Regulation and Disease.Biophysical journal · 2020Article
- Chloride promotes refolding of activeFEBS open bio · 2019Article
- A comprehensive ensemble model for comparing the allosteric effect of ordered and disordered proteins.PLoS computational biology · 2018Article
- Differential Substrate Recognition by Maltose Binding Proteins Influenced by Structure and Dynamics.Biochemistry · 2018Article
- Thermal Activity in Affinity Separation Techniques Such as Liquid-Liquid Extraction Analyzed by Isothermal Titration Calorimetry and Accuracy Analysis of the Technique in the Molar Concentration Domain.Industrial & engineering chemistry research · 2018Article
- Thermodynamic and NMR Assessment of Ligand Cooperativity and Intersubunit Communication in Symmetric Dimers: Application to Thymidylate Synthase.Frontiers in molecular biosciences · 2018Review
- Genetically tunable frustration controls allostery in an intrinsically disordered transcription factor.eLife · 2017Article
- Acetyl group coordinated progression through the catalytic cycle of an arylalkylamine N-acetyltransferase.PloS one · 2017Article
- Chemical shift imprint of intersubunit communication in a symmetric homodimer.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Comprehensive characterization of ligand-induced plasticity changes in a dimeric enzyme.The FEBS journal · 2016Article
- Dissecting Dynamic Allosteric Pathways Using Chemically Related Small-Molecule Activators.Structure (London, England : 1993) · 2016Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Allostery has been studied for many decades, yet it remains challenging to determine experimentally how it occurs at a molecular level. We have developed an approach combining isothermal titration calorimetry, circular dichroism and nuclear magnetic resonance spectroscopy to quantify allostery in terms of protein thermodynamics, structure and dynamics. This strategy was applied to study the interaction between aminoglycoside N-(6')-acetyltransferase-Ii and one of its substrates, acetyl coenzyme A. It was found that homotropic allostery between the two active sites of the homodimeric enzyme is modulated by opposing mechanisms. One follows a classical Koshland-Némethy-Filmer (KNF) paradigm, whereas the other follows a recently proposed mechanism in which partial unfolding of the subunits is coupled to ligand binding. Competition between folding, binding and conformational changes represents a new way to govern energetic communication between binding sites.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.