ArticleFrontiers in molecular biosciences2018
Millisecond Timescale Motions Connect Amino Acid Interaction Networks in Alpha Tryptophan Synthase.
Article in Frontiers in molecular biosciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 6 citations in OpenAlex.
- Solution-state nuclear magnetic resonance studies of theBiochemistry and biophysics reports · 2026Article
- Distinct conformational dynamics and allosteric networks in alpha tryptophan synthase during active catalysis.Protein science : a publication of the Protein Society · 2021Article
- Substitution of a Surface-Exposed Residue Involved in an Allosteric Network Enhances Tryptophan Synthase Function in Cells.Frontiers in molecular biosciences · 2021Article
- Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase α-subunit from solution-state NMR.Journal of biomolecular NMR · 2020Article
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5 authors at 1 institution in 1 country.
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Abstract
Tryptophan synthase is a model system for understanding allosteric regulation within enzyme complexes. Amino acid interaction networks were previously delineated in the isolated alpha subunit (αTS) in the absence of the beta subunit (βTS). The amino acid interaction networks were different between the ligand-free enzyme and the enzyme actively catalyzing turnover. Previous X-ray crystallography studies indicated only minor localized changes when ligands bind αTS, and so, structural changes alone could not explain the changes to the amino acid interaction networks. We hypothesized that the network changes could instead be related to changes in conformational dynamics. As such, we conducted nuclear magnetic resonance relaxation studies on different substrate- and products-bound complexes of αTS. Specifically, we collected
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