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

ATP synthase: subunit-subunit interactions in the stator stalk.

Joachim Weber1

  • 1Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409-1061, USA. joachim.weber@ttuhsc.edu

Biochimica Et Biophysica Acta
|May 30, 2006
PubMed
Summary

The stator stalk in ATP synthase connects the Fo and F1 subcomplexes, enabling proton translocation and ATP synthesis. This review details its structure and subunit interactions, crucial for enzyme function.

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

The German National Strategy for Gene- and Cell-Based Therapies: Generating Impact by Employing a Novel Multi-Stakeholder Approach.

Human gene therapy·2026
Same author

Scaling Electronic Consent for Research Integrated into Clinical Routine Processes.

Studies in health technology and informatics·2026
Same author

The Advanced Confidentiality Engine as a Scalable Tool for the Pseudonymization of Biomedical Data in Translational Settings: Development and Usability Study.

Journal of medical Internet research·2025
Same author

Authors' Reply: The University Medicine Greifswald's Trusted Third Party Dispatcher: State-of-the-Art Perspective Into Comprehensive Architectures and Complex Research Workflows.

JMIR medical informatics·2024
Same author

The Arabidopsis U1 snRNP regulates mRNA 3'-end processing.

Nature plants·2024
Same author

Development of a Trusted Third Party at a Large University Hospital: Design and Implementation Study.

JMIR medical informatics·2024

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • ATP synthase couples proton flow through Fo to ATP synthesis/hydrolysis in F1 via subunit rotation.
  • The peripheral stator stalk maintains connection between static F1 and Fo subcomplexes, enduring strain during rotation.
  • The Escherichia coli stator stalk comprises b2delta subunits, while other organisms utilize three or four different subunits.

Purpose of the Study:

  • To review the current understanding of the ATP synthase stator stalk structure.
  • To discuss the interactions between stator stalk subunits and their role in enzyme function.
  • To highlight recent advances in characterizing stator stalk components and their affinities.

Main Methods:

  • Affinity measurements between individual stator stalk components.

Related Experiment Videos

  • Detailed analysis of the interaction between subunit delta (or OSCP) and the F1 subcomplex.
  • Structural analysis of the stator stalk and its subunit interfaces.
  • Main Results:

    • Recent studies have quantified the binding affinities within the stator stalk.
    • The interaction between delta/OSCP and F1 has been extensively analyzed.
    • The review synthesizes current knowledge on stator stalk structure and subunit dynamics.

    Conclusions:

    • The stator stalk is essential for coupling proton translocation and ATP synthesis in ATP synthase.
    • Understanding stator stalk structure and subunit interactions is key to elucidating enzyme mechanism.
    • Further research on stator stalk components will advance our knowledge of energy transduction.