ArticleBiochemistry2009
The flexibility of a distant loop modulates active site motion and product release in ribonuclease A.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 83 citations in OpenAlex.
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- A flexible, allosteric loop regulates protein activity and rewires electrostatics.Protein science : a publication of the Protein Society · 2025Article
- The Impact of Second-Shell Nucleotides on Ligand Specificity in Cyclic Dinucleotide Riboswitches.Biochemistry · 2024Article
- Sequence - dynamics - function relationships in protein tyrosine phosphatases.QRB discovery · 2024Article
- From random to rational: improving enzyme design through electric fields, second coordination sphere interactions, and conformational dynamics.Chemical science · 2023Review
- Loop dynamics and the evolution of enzyme activity.Nature reviews. Chemistry · 2023Review
- Conformational exchange divergence along the evolutionary pathway of eosinophil-associated ribonucleases.Structure (London, England : 1993) · 2023Article
- Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases.Chemical science · 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
- Significant Loop Motions in the SsoPTP Protein Tyrosine Phosphatase Allow for Dual General Acid Functionality.Biochemistry · 2021Article
- Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments.The journal of physical chemistry. A · 2021Article
- E. coli RNase I exhibits a strong Ca2+-dependent inherent double-stranded RNase activity.Nucleic acids research · 2021Article
- Structural and Evolutionary Analyses of PR-4 SUGARWINs Points to a Different Pattern of Protein Function.Frontiers in plant science · 2021Article
- Binding of a SolubleBiochemistry · 2020Article
- Enzyme dynamics: Looking beyond a single structure.ChemCatChem · 2020Article
- Antagonism between substitutions in β-lactamase explains a path not taken in the evolution of bacterial drug resistance.The Journal of biological chemistry · 2020Article
- Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding.Biochemistry · 2020Article
- Uncovering the Molecular Interactions in the Catalytic Loop That Modulate the Conformational Dynamics in Protein Tyrosine Phosphatase 1B.Journal of the American Chemical Society · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The role of the flexible loop 1 in protein conformational motion and in the dissociation of enzymatic product from ribonuclease A (RNase A) was investigated by creation of a chimeric enzyme in which a 6-residue loop 1 from the RNase A homologue, eosinophil cationic protein (ECP), replaced the 12-residue loop 1 in RNase A. The chimera (RNase A(ECP)) experiences only local perturbations in NMR backbone chemical shifts compared to WT RNase A. Many of the flexible residues that were previously identified in WT as involved in an important conformational change now experience no NMR-detected millisecond motions in the chimera. Likewise, binding of the product analogue, 3'-CMP, to RNase A(ECP) results in only minor chemical shift changes in the enzyme similar to what is observed for the H48A mutant of RNase A and in contrast to WT enzyme. For both RNase A(ECP) and H48A there is a 10-fold decrease in the product release rate constant, k(off), compared to WT, in agreement with previous studies indicating the importance of flexibility in RNase A in the overall rate-limiting product release step. Together, these NMR and biochemical experiments provide additional insight into the mechanism of millisecond motions in the RNase A catalytic cycle.
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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.