Jove
Visualize
Contact Us
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 Videos

Structural aspects of GroEL function

A Horovitz1

  • 1Department of Structural Biology, Weizmann Institute, Rehovot, Israel. csamnon@weizmann.weizmann.ac.il

Current Opinion in Structural Biology
|March 31, 1998
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Gynodioecy as a possible populational strategy for increasing reproductive output.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·2013
Same author

How an Ebstein-Barr virus may induce acute fulminant myocarditis in a young immunocompetent adult: a case report.

The West Indian medical journal·2013
Same author

Review: allostery in chaperonins.

Journal of structural biology·2001
Same author

Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1.

Protein science : a publication of the Protein Society·2001
Same author

In vivo and in vitro function of GroEL mutants with impaired allosteric properties.

The Journal of biological chemistry·2000
Same author

On the relationship between the Hill coefficients for steady-state and transient kinetic data: a criterion for concerted transitions in allosteric proteins.

Bulletin of mathematical biology·2000
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026
Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026
Same journal

Tuning the physicochemical properties of rationally designed protein-based biomolecular condensates.

Current opinion in structural biology·2026
See all related articles

The chaperonin GroEL and its cofactor GroES use ATP to help proteins fold. Structural studies reveal how GroEL

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Chaperonins like GroEL are essential molecular machines that assist protein folding.
  • Protein folding is a critical process for cellular function, and misfolding is linked to disease.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying the ATP-regulated protein folding function of the GroEL-GroES chaperonin system.
  • To provide atomic-level insights into the conformational changes GroEL undergoes during its functional cycle.

Main Methods:

  • X-ray crystallography was used to determine the structure of the GroEL.GroES.(ADP)7 complex.
  • Cryo-electron microscopy was employed to visualize allosteric states of GroEL in relation to ATP binding.
  • Peptide interaction studies utilized X-ray crystallography.

Related Experiment Videos

Main Results:

  • The crystal structure of the GroEL.GroES.(ADP)7 complex revealed distinct cavity lining properties in different functional states: hydrophobic in the polypeptide acceptor state and hydrophilic in the protein-release state.
  • Cryo-electron microscopy provided visualizations of GroEL's allosteric states modulated by ATP.
  • X-ray crystallography characterized the interaction between GroEL's apical domain and a bound peptide.

Conclusions:

  • The structural and functional data provide a detailed mechanistic understanding of how GroEL-GroES facilitates protein folding through ATP-dependent conformational changes.
  • The findings highlight the dynamic nature of the chaperonin cavity and its role in substrate binding and release.
  • This work advances our knowledge of molecular chaperones and their importance in maintaining proteostasis.