ArticleBiophysical journal2015
Disorder-to-Order Transition of an Active-Site Loop Mediates the Allosteric Activation of Sortase A.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration.Science (New York, N.Y.) · 2026Article
- Ensemble Docking as a Tool for the Rational Design of PeptidomimeticInternational journal of molecular sciences · 2024Article
- Re-Balancing Replica Exchange with Solute Tempering for Sampling Dynamic Protein Conformations.Journal of chemical theory and computation · 2023Article
- Theoretical Studies of Leu-Pro-Arg-Asp-Ala Pentapeptide (LPRDA) Binding to Sortase A ofMolecules (Basel, Switzerland) · 2022Article
- Advanced Sampling Methods for Multiscale Simulation of Disordered Proteins and Dynamic Interactions.Biomolecules · 2021Review
- Article
- Article
- Experimentally-driven protein structure modeling.Journal of proteomics · 2020Review
- Albumin Alters the Conformational Ensemble of Amyloid-β by Promiscuous Interactions: Implications for Amyloid Inhibition.Frontiers in molecular biosciences · 2020Article
- Disorder driven allosteric control of protein activity.Current research in structural biology · 2020Article
- Residual Structures and Transient Long-Range Interactions of p53 Transactivation Domain: Assessment of Explicit Solvent Protein Force Fields.Journal of chemical theory and computation · 2019Article
- Review
- Conversion of an amide to a high-energy thioester by Staphylococcus aureus sortase A is powered by variable binding affinity for calcium.Scientific reports · 2018Article
- Temperature-induced collapse of a disordered peptide observed by three sampling methods in molecular dynamics simulations.The Journal of chemical physics · 2018Article
- Tuning Free Energy by Backbone Conformational Entropy: A Strategy from Disordered Proteins.Biophysical journal · 2018Article
- Ca2+ binding induced sequential allosteric activation of sortase A: An example for ion-triggered conformational selection.PloS one · 2018Article
- Enhanced Sampling of Intrinsic Structural Heterogeneity of the BH3-Only Protein Binding Interface of Bcl-xL.The journal of physical chemistry. B · 2017Article
- Unidirectional allostery in the regulatory subunit RIα facilitates efficient deactivation of protein kinase A.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Protein Allostery and Conformational Dynamics.Chemical reviews · 2016Review
- Atomistic Glimpse of the Orderly Chaos of One Protein.Biophysical journal · 2015Article
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2 authors.
Funding
Abstract
Intrinsically disordered proteins and intrinsically disordered regions are implicated in many biological functions and associated with many diseases, but their conformational characterizations are challenging. The disordered β6/β7 loop of Staphylococcus aureus sortase A is involved in the binding of both sorting signals and calcium. Calcium binding allosterically activates the enzyme, but the detailed mechanism has been unclear. Here we adapted the replica exchange with solute tempering method to sample the conformations of the β6/β7 loop, in apo form and in three liganded forms (bound with a sorting signal or calcium or both). The extensive molecular dynamics simulations yield atomic details of the disordered-to-order transition of the loop and suggest a mechanism for allosteric activation: calcium binding results in partial closure and ordering of the loop, thereby leading to preorganization of the binding pocket for the sorting signal. The approach has general applicability to the study of intrinsically disordered regions.
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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.