ArticleNature communications2021
Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.
Article in Nature communications, 2021. 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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Who cites it
22 citing papers in PubMed.
- Site-Specific Features Guiding Effective Reversible Photocontrol of Tryptophan Synthase With the Unnatural Amino Acid AzoF.Chembiochem : a European journal of chemical biology · 2026Article
- In silico pathway-based subtractive proteomics for identifying novel drug targets in Candida albicans with structure-guided drug repurposing of aspartate-semialdehyde dehydrogenase inhibitors.Journal of molecular modeling · 2026Article
- Structural and molecular basis for allosteric regulation and catalytic coupling of human phosphoribosylformylglycinamidine synthase.Nature communications · 2026Article
- Boosting Reversible Photocontrol of a Photoxenase by an Engineered Conformational Shift.Angewandte Chemie (International ed. in English) · 2026Article
- Purine Chemistry in the Early RNA World at the Origins of Life: From RNA and Nucleobases Lesions to Current Key Metabolic Routes.Chembiochem : a European journal of chemical biology · 2025Review
- Activity Regulation of a Glutamine Amidotransferase Bienzyme Complex by Substrate-Induced Subunit Interface Expansion.ACS catalysis · 2025Article
- 3D variability analysis reveals a hidden conformational change controlling ammonia transport in human asparagine synthetase.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
- 3D Variability Analysis Reveals a Hidden Conformational Change Controlling Ammonia Transport in Human Asparagine Synthetase.bioRxiv : the preprint server for biology · 2024Article
- Article
- ATLAS: protein flexibility description from atomistic molecular dynamics simulations.Nucleic acids research · 2024Article
- Catalytic Effects of Active Site Conformational Change in the Allosteric Activation of Imidazole Glycerol Phosphate Synthase.ACS catalysis · 2023Article
- Connected Component Analysis of Dynamical Perturbation Contact Networks.The journal of physical chemistry. B · 2023Article
- 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
- Turning up the heat mimics allosteric signaling in imidazole-glycerol phosphate synthase.Nature communications · 2023Article
- Assessing the applicability ofJournal of biomolecular NMR · 2023Article
- Observation of conformational changes that underlie the catalytic cycle of Xrn2.Nature chemical biology · 2022Article
- Towards autonomous analysis of chemical exchange saturation transfer experiments using deep neural networks.Journal of biomolecular NMR · 2022Article
- Time Evolution of the Millisecond Allosteric Activation of Imidazole Glycerol Phosphate Synthase.Journal of the American Chemical Society · 2022Article
- Modeling Catalysis in Allosteric Enzymes: Capturing Conformational Consequences.Topics in catalysis · 2022Article
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Authors and funding
7 authors.
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Abstract
Imidazole glycerol phosphate synthase (HisFH) is a heterodimeric bienzyme complex operating at a central branch point of metabolism. HisFH is responsible for the HisH-catalyzed hydrolysis of glutamine to glutamate and ammonia, which is then used for a cyclase reaction by HisF. The HisFH complex is allosterically regulated but the underlying mechanism is not well understood. Here, we elucidate the molecular basis of the long range, allosteric activation of HisFH. We establish that the catalytically active HisFH conformation is only formed when the substrates of both HisH and HisF are bound. We show that in this conformation an oxyanion hole in the HisH active site is established, which rationalizes the observed 4500-fold allosteric activation compared to the inactive conformation. In solution, the inactive and active conformations are in a dynamic equilibrium and the HisFH turnover rates correlate with the population of the active conformation, which is in accordance with the ensemble model of allostery.
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