ArticleStructure (London, England : 1993)2016
Dissecting Dynamic Allosteric Pathways Using Chemically Related Small-Molecule Activators.
Article in Structure (London, England : 1993), 2016. 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.
- Facilitating NMR Resonance Assignment with Metabolic Tampering.bioRxiv : the preprint server for biology · 2026Article
- Boosting Reversible Photocontrol of a Photoxenase by an Engineered Conformational Shift.Angewandte Chemie (International ed. in English) · 2026Article
- Article
- Catalytic Effects of Active Site Conformational Change in the Allosteric Activation of Imidazole Glycerol Phosphate Synthase.ACS catalysis · 2023Article
- Turning up the heat mimics allosteric signaling in imidazole-glycerol phosphate synthase.Nature communications · 2023Article
- Article
- ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy.Science advances · 2022Article
- Time Evolution of the Millisecond Allosteric Activation of Imidazole Glycerol Phosphate Synthase.Journal of the American Chemical Society · 2022Article
- A simple method to determine changes in the affinity between HisF and HisH in the Imidazole Glycerol Phosphate Synthase heterodimer.PloS one · 2022Article
- Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.Nature communications · 2021Article
- Community Network Analysis of Allosteric Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Substitution of a Surface-Exposed Residue Involved in an Allosteric Network Enhances Tryptophan Synthase Function in Cells.Frontiers in molecular biosciences · 2021Article
- Regulation of MIF Enzymatic Activity by an Allosteric Site at the Central Solvent Channel.Cell chemical biology · 2020Article
- NMR and computational methods for molecular resolution of allosteric pathways in enzyme complexes.Biophysical reviews · 2020Review
- Light Regulation of Enzyme Allostery through Photo-responsive Unnatural Amino Acids.Cell chemical biology · 2019Article
- Exploring Allosteric Pathways of a V-Type Enzyme with Dynamical Perturbation Networks.The journal of physical chemistry. B · 2019Article
- Chemical Exchange.Methods in enzymology · 2019Article
- Eigenvector centrality for characterization of protein allosteric pathways.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- General Expressions for Carr-Purcell-Meiboom-Gill Relaxation Dispersion for N-Site Chemical Exchange.Biochemistry · 2018Article
- Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The allosteric mechanism of the heterodimeric enzyme imidazole glycerol phosphate synthase was studied in detail with solution nuclear magnetic resonance spectroscopy and molecular dynamics simulations. We studied IGPS in complex with a series of allosteric activators corresponding to a large range of catalytic rate enhancements (26- to 4,900-fold), in which ligand binding is entropically driven. Conformational flexibility on the millisecond timescale plays a crucial role in intersubunit communication. Carr-Purcell-Meiboom-Gill relaxation dispersion experiments probing Ile, Leu, and Val methyl groups reveal that the apo- and glutamine-mimicked complexes are static on the millisecond timescale. Domain-wide motions are stimulated in the presence of the allosteric activators. These studies, in conjunction with ligand titrations, demonstrate that the allosteric network is widely dispersed and varies with the identity of the effector. Furthermore, we find that stronger allosteric ligands create more conformational flexibility on the millisecond timescale throughout HisF. This domain-wide loosening leads to maximum catalytic activity.
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