Jove
Visualize
Contact Us

Related Concept Videos

Energy to Drive Translocation01:37

Energy to Drive Translocation

2.1K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
2.1K
ATP Synthase: Structure01:18

ATP Synthase: Structure

13.1K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
13.1K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.5K
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.
The...
18.5K
Mechanical Protein Functions01:58

Mechanical Protein Functions

5.1K
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
5.1K
Structural Protein Function01:56

Structural Protein Function

2.8K
2.8K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

5.9K
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.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Development and optimization of human T-cell leukemia virus-specific antibody-dependent cell-mediated cytotoxicity (ADCC) assay directed to the envelope protein.

Journal of virology·2025
Same author

The Properties and Domain Requirements for Phase Separation of the Sup35 Prion Protein In Vivo.

Biomolecules·2023
Same author

Overexpression of Hsp104 by Causing Dissolution of the Prion Seeds Cures the Yeast [<i>PSI</i>] Prion.

International journal of molecular sciences·2023
Same author

Nucleotide exchange is sufficient for Hsp90 functions in vivo.

Nature communications·2023
Same author

Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [<i>PSI</i>] Curing by Hsp104 Overexpression.

Molecular and cellular biology·2023
Same author

Human J-Domain Protein DnaJB6 Protects Yeast from [<i>PSI</i><sup>+</sup>] Prion Toxicity.

Biology·2022
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Video

Updated: Sep 14, 2025

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

18.6K

ATP plays a structural role in Hsp90 function.

Michael Reidy1, Daniel C Masison2

  • 1Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA. michael.reidy@nih.gov.

Nature Communications
|July 21, 2025
PubMed
Summary

Adenosine triphosphate (ATP) binding, not hydrolysis, is essential for Hsp90 chaperone function. ATP acts as a structural linker, stabilizing the Hsp90 clamp through interactions with arginine R380.

More Related Videos

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

5.8K
Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
11:22

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Published on: January 30, 2018

10.2K

Related Experiment Videos

Last Updated: Sep 14, 2025

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

18.6K
Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

5.8K
Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
11:22

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Published on: January 30, 2018

10.2K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Heat shock protein 90 (Hsp90) is a crucial molecular chaperone.
  • Hsp90 utilizes adenosine triphosphate (ATP) for its function.
  • The precise role of ATP binding versus hydrolysis in Hsp90's mechanism remains unclear.

Purpose of the Study:

  • To elucidate the structural role of ATP in Hsp90 chaperone function.
  • To investigate the interaction between ATP and conserved residues, specifically arginine R380.
  • To understand how ATP binding and hydrolysis influence Hsp90 clamp dynamics.

Main Methods:

  • The study likely involved structural biology techniques (e.g., X-ray crystallography, cryo-EM) to visualize Hsp90-ATP complexes.
  • Biochemical assays were probably used to assess the impact of ATP binding and hydrolysis on Hsp90 activity.
  • Mutagenesis studies targeting R380 may have been employed to test its functional significance.

Main Results:

  • Findings indicate that ATP binding, not hydrolysis, is critical for Hsp90's structural integrity and function.
  • The gamma phosphate of ATP repositions to interact with arginine R380, stabilizing the closed chaperone clamp.
  • ATP acts as a structural linker, tethering the N and M domains of Hsp90, with hydrolysis facilitating clamp reopening.

Conclusions:

  • The essential role of ATP in Hsp90 function is structural, serving to stabilize the closed clamp conformation.
  • Arginine R380 functions as an "arginine finger" by interacting with ATP, suggesting nucleotides can be structural elements in NTPase families.
  • This work provides new insights into the mechanism of Hsp90 and the broader role of nucleotides in protein-ligand interactions.