ArticleBiophysical journal2012
Force distribution reveals signal transduction in E. coli Hsp90.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Dynamic Coupling between Tom22 Motions and Tom40 Pore Dynamics Modulates Ion Transport in the Mitochondrial TOM Complex.Journal of chemical information and modeling · 2025Article
- The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding.Nature communications · 2024Article
- The Onset of Molecule-Spanning Dynamics in Heat Shock Protein Hsp90.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Insight into the Nucleotide Based Modulation of the Grp94 Molecular Chaperone Using Multiscale Dynamics.The journal of physical chemistry. B · 2023Article
- Hierarchical dynamics in allostery following ATP hydrolysis monitored by single molecule FRET measurements and MD simulations.Chemical science · 2021Article
- Autoregulation of von Willebrand factor function by a disulfide bond switch.Science advances · 2018Article
- One-Way Allosteric Communication between the Two Disulfide Bonds in Tissue Factor.Biophysical journal · 2017Article
- Article
- Access Path to the Ligand Binding Pocket May Play a Role in Xenobiotics Selection by AhR.PloS one · 2016Article
- Mapping Mechanical Force Propagation through Biomolecular Complexes.Nano letters · 2015Article
- Dynamic Allostery of the Catabolite Activator Protein Revealed by Interatomic Forces.PLoS computational biology · 2015Article
- Allosteric regulation of focal adhesion kinase by PIP₂ and ATP.Biophysical journal · 2015Article
- Computational modeling of allosteric regulation in the hsp90 chaperones: a statistical ensemble analysis of protein structure networks and allosteric communications.PLoS computational biology · 2014Article
- Allosteric regulation of the Hsp90 dynamics and stability by client recruiter cochaperones: protein structure network modeling.PloS one · 2014Article
- An allosteric signaling pathway of human 3-phosphoglycerate kinase from force distribution analysis.PLoS computational biology · 2014Article
- ATP-driven molecular chaperone machines.Biopolymers · 2013Review
- Time-resolved force distribution analysis.BMC biophysics · 2013Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-shock protein 90 (Hsp90) is an ubiquitous chaperone that is essential for cell function in that it promotes client-protein folding and stabilization. Its function is tightly controlled by an ATP-dependent large conformational transition between the open and closed states of the Hsp90 dimer. The underlying allosteric pathway has remained largely unknown, but it is revealed here in atomistic detail for the Escherichia coli homolog HtpG. Using force-distribution analysis based on molecular-dynamics simulations (>1 μs in total), we identify an internal signaling pathway that spans from the nucleotide-binding site to an ~2.3-nm-distant region in the HtpG middle domain, that serves as a dynamic hinge region, and to a putative client-protein-binding site in the middle domain. The force transmission is triggered by ATP capturing a magnesium ion and thereby rotating and bending a proximal long α-helix, which represents the major force channel into the middle domain. This allosteric mechanism is, with statistical significance, distinct from the dynamics in the ADP and apo states. Tracking the distribution of forces is likely to be a promising tool for understanding and guiding experiments of complex allosteric proteins in general.
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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.