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 changes in glycogen phosphorylase induced by phosphorylation.

S R Sprang1, K R Acharya, E J Goldsmith

  • 1Department of Biochemistry, University of Texas Southwestern Medical Centre, Dallas 75235-9050.

Nature
|November 17, 1988
PubMed
Summary

Phosphorylation of glycogen phosphorylase b at serine-14 triggers structural changes, initiating enzyme activation. These changes enhance subunit interactions and modify substrate and effector binding sites, crucial for glycogen metabolism regulation.

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

Evaluation of owner experiences and adherence to home-cooked diet recipes for dogs.

The Journal of small animal practice·2015
Same author

A micro-patterned silicon chip as sample holder for macromolecular crystallography experiments with minimal background scattering.

Scientific reports·2015
Same author

Structure based drug design of angiotensin-I converting enzyme inhibitors.

Current medicinal chemistry·2012
Same author

Cryopreservation of buffy-coat-derived platelet concentrates in dimethyl sulfoxide and platelet additive solution.

Cryobiology·2011
Same author

Genomics and structure/function studies of Rhabdoviridae proteins involved in replication and transcription.

Antiviral research·2010
Same author

The VIZIER project: preparedness against pathogenic RNA viruses.

Antiviral research·2007

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Glycogen phosphorylase is a key enzyme in glycogen metabolism.
  • Its activity is regulated by phosphorylation and allosteric effectors.
  • Understanding the structural basis of its activation is crucial for metabolic research.

Purpose of the Study:

  • To compare the refined crystal structures of dimeric glycogen phosphorylase b and a.
  • To elucidate the initial structural changes associated with enzyme activation.
  • To understand how phosphorylation at serine-14 impacts enzyme conformation and function.

Main Methods:

  • X-ray crystallography to determine and compare enzyme structures.
  • Structural analysis of dimeric glycogen phosphorylase b and a.

Related Experiment Videos

  • Comparative analysis of structural differences between the two enzyme forms.

    • Main Results:

    • Phosphorylation of serine-14 induces an ordered helical conformation in the N-terminus of each subunit.
    • The N-terminus binds to the dimer surface, initiating activation.
    • Structural alterations in N- and C-terminal regions strengthen inter-subunit interactions.
    • Changes modify the binding sites for allosteric effectors and substrates.

    Conclusions:

    • The structural changes observed upon serine-14 phosphorylation represent the first step in glycogen phosphorylase activation.
    • These conformational changes are critical for regulating enzyme activity and substrate binding.
    • The findings provide insights into the allosteric regulation mechanism of glycogen phosphorylase.