ArticleProceedings of the National Academy of Sciences of the United States of America2017
Nanomechanics of the substrate binding domain of Hsp70 determine its allosteric ATP-induced conformational change.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers.Biochemistry · 2025Review
- Single-molecule study of the dynamics of the molecular chaperone Hsp70 during the functional cycle.Biochemical Society transactions · 2025Review
- Prediction of the Stability of Protein Substructures Using AI/ML Techniques.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Looking at Biomolecular Interactions through the Lens of Correlated Fluorescence Microscopy and Optical Tweezers.International journal of molecular sciences · 2023Review
- Single-Molecule Optical Tweezers As a Tool for Delineating the Mechanisms of Protein-Processing Mechanoenzymes.ACS omega · 2023Review
- Direct observation of chemo-mechanical coupling in DnaK by single-molecule force experiments.Biophysical journal · 2022Article
- Capturing intrinsic nanomechanics of allostery.Biophysical journal · 2022Article
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Direct observation of chaperone-modulated talin mechanics with single-molecule resolution.Communications biology · 2022Article
- Allosteric Inter-Domain Contacts in Bacterial Hsp70 Are Located in Regions That Avoid Insertion and Deletion Events.International journal of molecular sciences · 2022Article
- Interpretation of Single-Molecule Force Experiments on Proteins Using Normal Mode Analysis.Nanomaterials (Basel, Switzerland) · 2021Article
- Classifying Residues in Mechanically Stable and Unstable Substructures Based on a Protein Sequence: The Case Study of the DnaK Hsp70 Chaperone.Nanomaterials (Basel, Switzerland) · 2021Article
- Studying protein folding in health and disease using biophysical approaches.Emerging topics in life sciences · 2021Article
- Studying heat shock proteins through single-molecule mechanical manipulation.Cell stress & chaperones · 2020Review
- Single-Molecule Mechanics in Ligand Concentration Gradient.Micromachines · 2020Article
- Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains.Nature communications · 2019Article
- On-the-Fly Calibrated Measure and Remote Control of Temperature and Viscosity at Nanoscale.ACS omega · 2018Article
- Unraveling the Mechanical Unfolding Pathways of a Multidomain Protein: Phosphoglycerate Kinase.Biophysical journal · 2018Article
- The β6/β7 region of the Hsp70 substrate-binding domain mediates heat-shock response and prion propagation.Cellular and molecular life sciences : CMLS · 2018Article
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6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Owing to the cooperativity of protein structures, it is often almost impossible to identify independent subunits, flexible regions, or hinges simply by visual inspection of static snapshots. Here, we use single-molecule force experiments and simulations to apply tension across the substrate binding domain (SBD) of heat shock protein 70 (Hsp70) to pinpoint mechanical units and flexible hinges. The SBD consists of two nanomechanical units matching 3D structural parts, called the α- and β-subdomain. We identified a flexible region within the rigid β-subdomain that gives way under load, thus opening up the α/β interface. In exactly this region, structural changes occur in the ATP-induced opening of Hsp70 to allow substrate exchange. Our results show that the SBD's ability to undergo large conformational changes is already encoded by passive mechanics of the individual elements.
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