ArticleScientific reports2017
Conserved amino acid networks modulate discrete functional properties in an enzyme superfamily.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Statistical Coupling Analysis Predicts Correlated Motions in Dihydrofolate Reductase.The journal of physical chemistry. B · 2024Article
- Clustering protein functional families at large scale with hierarchical approaches.Protein science : a publication of the Protein Society · 2024Article
- Statistical Coupling Analysis Predicts Correlated Motions in Dihydrofolate Reductase.bioRxiv : the preprint server for biology · 2024Article
- Exploring Oxidoreductases from Extremophiles for Biosynthesis in a Non-Aqueous System.International journal of molecular sciences · 2023Review
- Undersampling and the inference of coevolution in proteins.Cell systems · 2023Article
- Conformational exchange divergence along the evolutionary pathway of eosinophil-associated ribonucleases.Structure (London, England : 1993) · 2023Article
- Identifying structural and dynamic changes during the Biliverdin Reductase B catalytic cycle.Frontiers in molecular biosciences · 2023Article
- Fundamentals to function: Quantitative and scalable approaches for measuring protein stability.Cell systems · 2021Review
- Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding.Biochemistry · 2020Article
- Mechanisms of Specific versus Nonspecific Interactions of Aggregation-Prone Inhibitors and Attenuators.Journal of medicinal chemistry · 2019Article
- Evolutionary Trends in RNA Base Selectivity Within the RNase A Superfamily.Frontiers in pharmacology · 2019Article
- Modulating Enzyme Activity by Altering Protein Dynamics with Solvent.Biochemistry · 2018Article
- Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018Review
- Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily.Structure (London, England : 1993) · 2018Article
- Ligand-Induced Variations in Structural and Dynamical Properties Within an Enzyme Superfamily.Frontiers in molecular biosciences · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
In this work, we applied the sequence-based statistical coupling analysis approach to characterize conserved amino acid networks important for biochemical function in the pancreatic-type ribonuclease (ptRNase) superfamily. This superfamily-wide analysis indicates a decomposition of the RNase tertiary structure into spatially distributed yet physically connected networks of co-evolving amino acids, termed sectors. Comparison of this statistics-based description with new NMR experiments data shows that discrete amino acid networks, termed sectors, control the tuning of distinct functional properties in different enzyme homologs. Further, experimental characterization of evolutionarily distant sequences reveals that sequence variation at sector positions can distinguish homologs with a conserved dynamic pattern and optimal catalytic activity from those with altered dynamics and diminished catalytic activities. Taken together, these results provide important insights into the mechanistic design of the ptRNase superfamily, and presents a structural basis for evolutionary tuning of function in functionally diverse enzyme homologs.
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