ArticleBiophysical journal2005
Structural elements in IGP synthase exclude water to optimize ammonia transfer.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 45 citations in OpenAlex.
- 3D variability analysis reveals a hidden conformational change controlling ammonia transport in human asparagine synthetase.Nature communications · 2024Article
- 3D Variability Analysis Reveals a Hidden Conformational Change Controlling Ammonia Transport in Human Asparagine Synthetase.bioRxiv : the preprint server for biology · 2024Article
- Time Evolution of the Millisecond Allosteric Activation of Imidazole Glycerol Phosphate Synthase.Journal of the American Chemical Society · 2022Article
- Distinct allosteric pathways in imidazole glycerol phosphate synthase from yeast and bacteria.Biophysical journal · 2022Article
- Allosteric regulation of substrate channeling:Frontiers in molecular biosciences · 2022Review
- Allosteric Communication Disrupted by a Small Molecule Binding to the Imidazole Glycerol Phosphate Synthase Protein-Protein Interface.Biochemistry · 2016Article
- Visualizing the tunnel in tryptophan synthase with crystallography: Insights into a selective filter for accommodating indole and rejecting water.Biochimica et biophysica acta · 2016Article
- Conformational changes involving ammonia tunnel formation and allosteric control in GMP synthetase.Archives of biochemistry and biophysics · 2014Article
- Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum.Microbial biotechnology · 2014Review
- Gates of enzymes.Chemical reviews · 2013Review
- Substrate activation and conformational dynamics of guanosine 5'-monophosphate synthetase.Biochemistry · 2013Article
- Exploring residue component contributions to dynamical network models of allostery.Journal of chemical theory and computation · 2012Article
- Allosteric pathways in imidazole glycerol phosphate synthase.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
- The interaction of ammonia and xenon with the imidazole glycerol phosphate synthase from Thermotoga maritima as detected by NMR spectroscopy.Protein science : a publication of the Protein Society · 2010Article
- Carbamate transport in carbamoyl phosphate synthetase: a theoretical and experimental investigation.Journal of the American Chemical Society · 2010Article
- Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima.Journal of biomolecular NMR · 2009Article
- Biosynthesis of Histidine.EcoSal Plus · 2009Article
- Solvent reaction field potential inside an uncharged globular protein: a bridge between implicit and explicit solvent models?The Journal of chemical physics · 2007Article
- Structure of a bacterial pyridoxal 5'-phosphate synthase complex.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In the complex pathway of histidine biosynthesis, a key branch point linking amino acid and purine biosynthesis is catalyzed by the bifunctional enzyme imidazole glycerol phosphate (IGP) synthase. The first domain of IGP synthase, a triad glutamine amidotransferase, hydrolyzes glutamine to form glutamate and ammonia. Its activity is tightly regulated by the binding of the substrate PRFAR to its partner synthase domain. Recent crystal structures and molecular dynamics simulations strongly suggest that the synthase domain, a (beta/alpha)(8) barrel protein, mediates the insertion of ammonia and ring formation in IGP by channeling ammonia from one remote active site to the other. Here, we combine both mutagenesis experiments and computational investigations to gain insight into the transfer of ammonia and the mechanism of conduction. We discover an alternate route for the entrance of ammonia into the (beta/alpha)(8) barrel and argue that water acts as both agonist and antagonist to the enzymatic function. Our results indicate that the architecture of the two subdomains, most notably the strict conservation of key residues at the interface and within the (beta/alpha)(8) barrel, has been optimized to allow the efficient passage of ammonia, and not water, between the two remote active 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.