ArticlePLoS computational biology2010
The role of oligomerization and cooperative regulation in protein function: the case of tryptophan synthase.
Article in PLoS computational biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- Negative allosteric regulation of protein arginine methyltransferase 1 (PRMT1) through half-of-sites reactivity.The Journal of biological chemistry · 2026Article
- Human CTR1 Through the Ages: Milestones and Emerging Roles in Disease and Therapy.Biomolecules · 2025Review
- Efficient identification of new small molecules targeting succinate dehydrogenase in non-small cell lung cancer.Cancer cell international · 2025Article
- Salmonella YqiC exerts its function through an oligomeric state.Protein science : a publication of the Protein Society · 2023Article
- Computational Analysis on the Allostery of Tryptophan Synthase: Relationship between α/β-Ligand Binding and Distal Domain Closure.The journal of physical chemistry. B · 2022Article
- Discovery of antimicrobial agent targeting tryptophan synthase.Protein science : a publication of the Protein Society · 2022Article
- Structural Basis for Allostery in PLP-dependent Enzymes.Frontiers in molecular biosciences · 2022Review
- Allosteric regulation of substrate channeling:Frontiers in molecular biosciences · 2022Review
- Human FoxP Transcription Factors as Tractable Models of the Evolution and Functional Outcomes of Three-Dimensional Domain Swapping.International journal of molecular sciences · 2021Review
- Human Cellular Retinol Binding Protein II Forms a Domain-Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering.Chembiochem : a European journal of chemical biology · 2020Article
- Protein oligomerization as a metabolic control mechanism: Application to apoE.Protein science : a publication of the Protein Society · 2019Article
- Relapsed acute lymphoblastic leukemia-specific mutations in NT5C2 cluster into hotspots driving intersubunit stimulation.Leukemia · 2018Article
- Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018Review
- Millisecond Timescale Motions Connect Amino Acid Interaction Networks in Alpha Tryptophan Synthase.Frontiers in molecular biosciences · 2018Article
- Article
- Investigation of Structural Dynamics of Enzymes and Protonation States of Substrates Using Computational Tools.Catalysts (Basel, Switzerland) · 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
- Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana.Frontiers in plant science · 2016Article
- Severing of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase.Protein science : a publication of the Protein Society · 2015Article
- Human and viral Golgi anti-apoptotic proteins (GAAPs) oligomerize via different mechanisms and monomeric GAAP inhibits apoptosis and modulates calcium.The Journal of biological chemistry · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The oligomerization/co-localization of protein complexes and their cooperative regulation in protein function is a key feature in many biological systems. The synergistic regulation in different subunits often enhances the functional properties of the multi-enzyme complex. The present study used molecular dynamics and Brownian dynamics simulations to study the effects of allostery, oligomerization and intermediate channeling on enhancing the protein function of tryptophan synthase (TRPS). TRPS uses a set of α/β-dimeric units to catalyze the last two steps of L-tryptophan biosynthesis, and the rate is remarkably slower in the isolated monomers. Our work shows that without their binding partner, the isolated monomers are stable and more rigid. The substrates can form fairly stable interactions with the protein in both forms when the protein reaches the final ligand-bound conformations. Our simulations also revealed that the α/β-dimeric unit stabilizes the substrate-protein conformation in the ligand binding process, which lowers the conformation transition barrier and helps the protein conformations shift from an open/inactive form to a closed/active form. Brownian dynamics simulations with a coarse-grained model illustrate how protein conformations affect substrate channeling. The results highlight the complex roles of protein oligomerization and the fine balance between rigidity and dynamics in protein function.
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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.