ArticleProceedings of the National Academy of Sciences of the United States of America1999
The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 114 citations in OpenAlex.
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- Catalytic Effects of Active Site Conformational Change in the Allosteric Activation of Imidazole Glycerol Phosphate Synthase.ACS catalysis · 2023Article
- Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.Microbial cell factories · 2023Review
- Extensive Summary of the Important Roles of Indole Propionic Acid, a Gut Microbial Metabolite in Host Health and Disease.Nutrients · 2022Review
- Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.Nature communications · 2021Article
- Revitalizing antifolates through understanding mechanisms that govern susceptibility and resistance.MedChemComm · 2019Review
- Unraveling the Structure and Mechanism of the MST(ery) Enzymes.Trends in biochemical sciences · 2018Review
- First insights of peptidoglycan amidation in Gram-positive bacteria - the high-resolution crystal structure of Staphylococcus aureus glutamine amidotransferase GatD.Scientific reports · 2018Article
- Synthesis of novel ligands targeting phenazine biosynthesis proteins as a strategy for antibiotic intervention.Monatshefte fur chemie · 2018Article
- Simultaneous identification of specifically interacting paralogs and interprotein contacts by direct coupling analysis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Inter-Protein Sequence Co-Evolution Predicts Known Physical Interactions in Bacterial Ribosomes and the Trp Operon.PloS one · 2016Article
- Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategy.Biochimica et biophysica acta · 2015Review
- The fused anthranilate synthase from Streptomyces venezuelae functions as a monomer.Molecular and cellular biochemistry · 2015Article
- Why do Sequence Signatures Predict Enzyme Mechanism? Homology versus Chemistry.Evolutionary bioinformatics online · 2015Article
- The structural biology of phenazine biosynthesis.Current opinion in structural biology · 2014Review
- Conformational changes involving ammonia tunnel formation and allosteric control in GMP synthetase.Archives of biochemistry and biophysics · 2014Article
- Article
- Allosteric pathways in imidazole glycerol phosphate synthase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anthranilate synthase catalyzes the synthesis of anthranilate from chorismate and glutamine and is feedback-inhibited by tryptophan. The enzyme of the hyperthermophile Sulfolobus solfataricus has been crystallized in the absence of physiological ligands, and its three-dimensional structure has been determined at 2.5-A resolution with x-ray crystallography. It is a heterotetramer of anthranilate synthase (TrpE) and glutamine amidotransferase (TrpG) subunits, in which two TrpG:TrpE protomers associate mainly via the TrpG subunits. The small TrpG subunit (195 residues) has the known "triad" glutamine amidotransferase fold. The large TrpE subunit (421 residues) has a novel fold. It displays a cleft between two domains, the tips of which contact the TrpG subunit across its active site. Clusters of catalytically essential residues are located inside the cleft, spatially separated from clustered residues involved in feedback inhibition. The structure suggests a model in which chorismate binding triggers a relative movement of the two domain tips of the TrpE subunit, activating the TrpG subunit and creating a channel for passage of ammonia toward the active site of the TrpE subunit. Tryptophan presumably blocks this rearrangement, thus stabilizing the inactive states of both subunits. The structure of the TrpE subunit is a likely prototype for the related enzymes 4-amino 4-deoxychorismate synthase and isochorismate synthase.
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