ArticleJournal of biomolecular NMR2009
Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima.
Article in Journal of biomolecular NMR, 2009. 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, 33 citations in OpenAlex.
- Remote allosteric control of single-atom Cu sites in Zr-MOFs enables selective CHScience advances · 2026Article
- Illuminating Protein Allostery by Chemically Accurate Contact Response Analysis (ChACRA).Journal of chemical theory and computation · 2024Article
- 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
- Role of a high centrality residue in protein dynamics and thermal stability.Journal of structural biology · 2021Article
- 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
- Propagation of the Allosteric Signal in Phosphofructokinase fromBiochemistry · 2019Article
- Accelerating 2D NMR relaxation dispersion experiments using iterated maps.Journal of biomolecular NMR · 2019Article
- Glutamine Hydrolysis by Imidazole Glycerol Phosphate Synthase Displays Temperature Dependent Allosteric Activation.Frontiers in molecular biosciences · 2018Article
- Altering the allosteric pathway in IGPS suppresses millisecond motions and catalytic activity.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Allosteric Communication Disrupted by a Small Molecule Binding to the Imidazole Glycerol Phosphate Synthase Protein-Protein Interface.Biochemistry · 2016Article
- Dissecting Dynamic Allosteric Pathways Using Chemically Related Small-Molecule Activators.Structure (London, England : 1993) · 2016Article
- Solution NMR Spectroscopy for the Study of Enzyme Allostery.Chemical reviews · 2016Review
- Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function.Progress in nuclear magnetic resonance spectroscopy · 2016Review
- Loop-loop interactions govern multiple steps in indole-3-glycerol phosphate synthase catalysis.Protein science : a publication of the Protein Society · 2014Article
- Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.Journal of biomolecular NMR · 2013Article
- What's in your buffer? Solute altered millisecond motions detected by solution NMR.Biochemistry · 2013Article
- Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Nanometer propagation of millisecond motions in V-type allostery.Structure (London, England : 1993) · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
IGPS is a 51 kDa heterodimeric enzyme comprised of two proteins, HisH and HisF, that catalyze the hydrolysis of glutamine to produce NH(3) in the HisH active site and the cyclization of ammonia with N'-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide (PRFAR) in HisF to produce imidazole glycerol phosphate (IGP) and 5-aminoimidazole-4-carboxamide ribotide (AICAR). Binding of PRFAR and IGP stimulates glutaminase activity in the HisH enzyme over 5,000 and 100-fold, respectively, despite the active sites being >25 A apart. The details of this long-range protein communication process were investigated by solution NMR spectroscopy and CPMG relaxation dispersion experiments. Formation of the heterodimer enzyme results in a reduction in millisecond motions in HisF that extend throughout the protein. Binding of lGP results in an increase in protein-wide millisecond dynamics evidenced as severe NMR line broadening and elevated R (ex) values. Together, these data demonstrate a grouping of flexible residues that link the HisF active site with the protein interface to which HisH binds and provide a model for the path of communication between the IGPS active sites.
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