ArticleStructure (London, England : 1993)2015
Perturbation of the Conformational Dynamics of an Active-Site Loop Alters Enzyme Activity.
Article in Structure (London, England : 1993), 2015. 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.
- Engineering human RNase 7 with an eosinophil RNase segment reveals determinants of cytotoxic and antimicrobial activity.The Journal of biological chemistry · 2026Article
- Origins of Catalysis in Non-Heme Fe(II)/2-Oxoglutarate-Dependent Histone Lysine Demethylase KDM4A with Differently Methylated Histone H3 Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Motif-VI loop acts as a nucleotide valve in the West Nile Virus NS3 Helicase.Nucleic acids research · 2024Article
- Non-active Site Residue in Loop L4 Alters Substrate Capture and Product Release in d-Arginine Dehydrogenase.Biochemistry · 2023Article
- Conformational exchange divergence along the evolutionary pathway of eosinophil-associated ribonucleases.Structure (London, England : 1993) · 2023Article
- Protein dynamics: The future is bright and complicated!Structural dynamics (Melville, N.Y.) · 2023Article
- Leveraging intrinsic flexibility to engineer enhanced enzyme catalytic activity.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Exploring the RNase A scaffold to combine catalytic and antimicrobial activities. Structural characterization of RNase 3/1 chimeras.Frontiers in molecular biosciences · 2022Article
- Structure-Based Design of an RNase Chimera for Antimicrobial Therapy.International journal of molecular sciences · 2021Article
- Recent advances in user-friendly computational tools to engineer protein function.Briefings in bioinformatics · 2021Review
- The Enzyme-Free Release of Nucleotides from Phosphoramidates Depends Strongly on the Amino Acid.Angewandte Chemie (International ed. in English) · 2020Article
- Enzyme dynamics: Looking beyond a single structure.ChemCatChem · 2020Article
- Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding.Biochemistry · 2020Article
- A computational study of the molecular basis of antibiotic resistance in a DXR mutant.Journal of computer-aided molecular design · 2019Article
- The Structural Dynamics of Engineered β-Lactamases Vary Broadly on Three Timescales yet Sustain Native Function.Scientific reports · 2019Article
- Evolutionary Trends in RNA Base Selectivity Within the RNase A Superfamily.Frontiers in pharmacology · 2019Article
- Testing a Human Antimicrobial RNase Chimera Against Bacterial Resistance.Frontiers in microbiology · 2019Article
- Ligand-Induced Variations in Structural and Dynamical Properties Within an Enzyme Superfamily.Frontiers in molecular biosciences · 2018Article
- Sequence-specific backbone resonance assignments and microsecond timescale molecular dynamics simulation of human eosinophil-derived neurotoxin.Biomolecular NMR assignments · 2017Article
- Applications of NMR and computational methodologies to study protein dynamics.Archives of biochemistry and biophysics · 2017Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The role of internal dynamics in enzyme function is highly debated. Specifically, how small changes in structure far away from the reaction site alter protein dynamics and overall enzyme mechanisms is of wide interest in protein engineering. Using RNase A as a model, we demonstrate that elimination of a single methyl group located >10 Å away from the reaction site significantly alters conformational integrity and binding properties of the enzyme. This A109G mutation does not perturb structure or thermodynamic stability, both in the apo and ligand-bound states. However, significant enhancement in conformational dynamics was observed for the bound variant, as probed over nano- to millisecond timescales, resulting in major ligand repositioning. These results illustrate the large effects caused by small changes in structure on long-range conformational dynamics and ligand specificities within proteins, further supporting the importance of preserving wild-type dynamics in enzyme systems that rely on flexibility for function.
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Registered trials
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.