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

C2 domain conformational changes in phospholipase C-delta 1

J A Grobler1, L O Essen, R L Williams

  • 1Laboratory of Molecular Biology, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0580, USA.

Nature Structural Biology
|September 1, 1996
PubMed
Summary

The structure of rat phospholipase C-delta 1 reveals how calcium binding to the C2 domain triggers a conformational change. This opening allows the enzyme to bind phospholipid headgroups, crucial for its 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

Long-acting formulations for the treatment of latent tuberculous infection: opportunities and challenges.

The international journal of tuberculosis and lung disease : the official journal of the International Union against Tuberculosis and Lung Disease·2018
Same author

Characterizing Class-Specific Exposure-Viral Load Suppression Response of HIV Antiretrovirals Using A Model-Based Meta-Analysis.

Clinical and translational science·2016
Same author

N- and P/Q-type Ca2+ channels in adrenal chromaffin cells.

Acta physiologica (Oxford, England)·2007
Same author

Light-driven DNA repair by photolyases.

Cellular and molecular life sciences : CMLS·2006
Same author

G-protein-coupled receptors for light: the three-dimensional structure of rhodopsin.

Chembiochem : a European journal of chemical biology·2002
Same author

Recognizing phosphatidylinositol 3-phosphate.

Cell·2001

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Phosphoinositide-specific phospholipase C-delta 1 (PLCδ1) is a key enzyme in signal transduction.
  • Understanding the structural basis of PLCδ1's enzymatic activity is crucial for deciphering cellular signaling pathways.

Purpose of the Study:

  • To determine the high-resolution crystal structure of the PH-domain truncated core of rat PLCδ1.
  • To compare this structure with a previously determined crystal form.
  • To elucidate the mechanism of calcium-dependent phospholipid binding.

Main Methods:

  • X-ray crystallography at 2.4 Å resolution.
  • Structural comparison of different crystal forms.
  • Analysis of Sm3+ (a Ca2+ analogue) binding sites and induced conformational changes.

Related Experiment Videos

Main Results:

  • The stereochemical relationship between the EF, catalytic, and C2 domains is conserved across different crystal forms.
  • Samarium ions (Sm3+) bind to two sites within the C2 domain's jaws.
  • Sm3+ binding displaces lysine residues and induces a conformational change, opening the C2 domain jaws by 9 Å to accommodate a phospholipid headgroup.

Conclusions:

  • The structure reveals a calcium-induced conformational change mechanism in the C2 domain of PLCδ1.
  • This conformational flexibility is essential for the enzyme's ability to bind phospholipid substrates.
  • The findings provide atomic-level insights into the regulation of PLCδ1 activity.