ArticleProceedings of the National Academy of Sciences of the United States of America2020
Analysis of allosteric communication in a multienzyme complex by ancestral sequence reconstruction.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. 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, 46 citations in OpenAlex.
- Functional conservation with mechanistic drift: AMP activation in the evolution of archaeal sugar kinases.Molecular biology and evolution · 2026Article
- Origins of allostery in vertebrate hemoglobin evolution.bioRxiv : the preprint server for biology · 2026Article
- Sequence-based generative AI design of versatile tryptophan synthases.Nature communications · 2026Article
- Functional and structural characterization of FProtein science : a publication of the Protein Society · 2025Article
- A naturally occurring standalone TrpB enzyme provides insights into allosteric communication within tryptophan synthase.Protein science : a publication of the Protein Society · 2025Article
- Insights into the low-temperature adaptation of an enzyme as studied through ancestral sequence reconstruction.Protein science : a publication of the Protein Society · 2025Article
- Altering Active-Site Loop Dynamics Enhances Standalone Activity of the Tryptophan Synthase Alpha Subunit.ACS catalysis · 2024Article
- Harnessing conformational dynamics in enzyme catalysis to achieve nature-like catalytic efficiencies: the shortest path map tool for computational enzyme redesign.Faraday discussions · 2024Article
- Ancestral Reconstruction and the Evolution of Protein Energy Landscapes.Annual review of biophysics · 2024Review
- Improving the Activity of Tryptophan Synthetase via a Nucleic Acid Scaffold.Molecules (Basel, Switzerland) · 2023Article
- A tale of two copies: Evolutionary trajectories of moth pheromone receptors.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Simple mechanisms for the evolution of protein complexity.Protein science : a publication of the Protein Society · 2022Review
- Estimating conformational heterogeneity of tryptophan synthase with a template-based Alphafold2 approach.Protein science : a publication of the Protein Society · 2022Article
- Protein Conformational Space at the Edge of Allostery: Turning a Nonallosteric Malate Dehydrogenase into an "Allosterized" Enzyme Using Evolution-Guided Punctual Mutations.Molecular biology and evolution · 2022Article
- Design and engineering of allosteric communications in proteins.Current opinion in structural biology · 2022Review
- A Model for Allosteric Communication in Drug Transport by the AcrAB-TolC Tripartite Efflux Pump.Antibiotics (Basel, Switzerland) · 2022Article
- Allosteric regulation of substrate channeling:Frontiers in molecular biosciences · 2022Review
- Article
- Ancestral lysosomal enzymes with increased activity harbor therapeutic potential for treatment of Hunter syndrome.iScience · 2021Article
- Tryptophan Synthase: Biocatalyst Extraordinaire.Chembiochem : a European journal of chemical biology · 2021Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tryptophan synthase (TS) is a heterotetrameric αββα complex. It is characterized by the channeling of the reaction intermediate indole and the mutual activation of the α-subunit TrpA and the β-subunit TrpB via a complex allosteric network. We have analyzed this allosteric network by means of ancestral sequence reconstruction (ASR), which is an in silico method to resurrect extinct ancestors of modern proteins. Previously, the sequences of TrpA and TrpB from the last bacterial common ancestor (LBCA) have been computed by means of ASR and characterized. LBCA-TS is similar to modern TS by forming a αββα complex with indole channeling taking place. However, LBCA-TrpA allosterically decreases the activity of LBCA-TrpB, whereas, for example, the modern ncTrpA from
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