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Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Updated: Feb 24, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Substrate-binding domain conformational dynamics mediate Hsp70 allostery.

Anastasia Zhuravleva1, Lila M Gierasch2

  • 1Astbury Centre for Structural Molecular Biology and Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom; a.zhuravleva@leeds.ac.uk gierasch@biochem.umass.edu.

Proceedings of the National Academy of Sciences of the United States of America
|June 4, 2015
PubMed
Summary
This summary is machine-generated.

Heat shock protein 70 (Hsp70) uses ATP binding to alter its structure, enhancing protein folding. Conformational changes in the substrate-binding domain are key to Hsp70

Keywords:
NMR chemical shift perturbationsconformational selectionentropically driven allosterymolecular chaperoneprotein quality control

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Heat shock protein 70 (Hsp70) chaperones bind ATP, reducing substrate affinity.
  • ATP binding induces N-terminal nucleotide-binding domain (NBD) and C-terminal substrate-binding domain (SBD) interactions.
  • Existing models don't fully explain Hsp70's allosteric regulation of substrate binding.

Purpose of the Study:

  • Investigate the allosteric mechanism of Hsp70 regulation.
  • Elucidate the role of conformational dynamics in Hsp70 function.
  • Understand how Hsp70 modulates substrate binding affinity and kinetics.

Main Methods:

  • Multifaceted study of Escherichia coli Hsp70 DnaK.
  • Analysis of conformational dynamics within the SBD.
  • Investigation of interdomain communication pathways.

Main Results:

  • Conformational dynamics in the SBD are crucial for Hsp70 allosteric regulation.
  • ATP binding promotes NBD-SBD interactions at specific sites.
  • Structural changes disrupt hydrophobic interactions, enhancing SBD dynamics and plasticity.

Conclusions:

  • Allosteric communication in Hsp70 involves dynamic changes within the SBD.
  • Negative, entropically driven allostery allows Hsp70 to bind diverse clients with precise control.
  • This mechanism confers plasticity for client binding without compromising interaction kinetics.