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

A structural model for GroEL-polypeptide recognition

A M Buckle1, R Zahn, A R Fersht

  • 1Cambridge University Chemical Laboratory, Medical Research Council Centre, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|April 15, 1997
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

Structural and dynamic requirements for optimal activity of the essential bacterial enzyme dihydrodipicolinate synthase.

PLoS computational biology·2012
Same author

Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73.

Oncogene·2010
Same author

The accessory subunit of mitochondrial DNA polymerase gamma determines the DNA content of mitochondrial nucleoids in human cultured cells.

Nucleic acids research·2009
Same author

Regulation by phosphorylation of the relative affinities of the N-terminal transactivation domains of p53 for p300 domains and Mdm2.

Oncogene·2009
Same author

Time-resolved fluorescence resonance energy transfer study shows a compact denatured state of the B domain of protein A.

Biochemistry·2009
Same author

Structure-function-rescue: the diverse nature of common p53 cancer mutants.

Oncogene·2007
Same journal

Chemotactic self-organization captures the dynamics of mammalian hair follicle patterning.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Tomographic imaging of superconducting order using particle-hole interference.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Inhibitory potential of autologous neutralizing antibodies sets quantitative limits on the rebound-competent HIV-1 reservoir.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Inferring epidemiological parameters under an infectious phylogeography model with visitor dynamics.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Analytical modeling for suction cup designs for skin-interfaced wearable devices.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Improving cell-free metabolism through direct integration of artificial respiratory chains.

Proceedings of the National Academy of Sciences of the United States of America·2026
See all related articles

A mini-chaperone, a peptide fragment of GroEL (chaperonin), shows functional activity. Its crystal structure reveals how it binds substrates, acting as an "unfoldase" by promoting protein unfolding.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • GroEL (chaperonin) is essential for protein folding in vivo.
  • Understanding GroEL's mechanism requires detailed structural insights into substrate binding.

Purpose of the Study:

  • To elucidate the structural basis of substrate binding and chaperoning activity using a GroEL mini-chaperone.
  • To investigate the role of GroEL in protein unfolding.

Main Methods:

  • Crystal structure determination of GroEL(191-376) mini-chaperone with an N-terminal tag at 1.7 A resolution.
  • Analysis of substrate-binding site interactions, including conformation and hydrogen bonding.

Main Results:

  • The crystal structure revealed an N-terminal tag mimicking peptide substrate binding in the active site.

Related Experiment Videos

  • Substrate peptides adopt an extended conformation, with predominantly hydrophobic interactions and four main-chain hydrogen bonds.
  • The GroEL active site exhibits flexibility, accommodating hydrophobic surfaces and molten globule states, supporting an "unfoldase" role.

    • Conclusions:

    • The GroEL mini-chaperone structure provides a model for understanding peptide substrate binding and GroEL's unfoldase activity.
    • The study highlights the importance of hydrophobic interactions and active site flexibility in GroEL's function.
    • A ring of connected binding sites in GroEL is proposed to explain substrate binding and activity.