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

Structure and function of carnitine acyltransferases.

Gerwald Jogl1, Yu-Shan Hsiao, Liang Tong

  • 1Department of Biological Sciences, Columbia University, New York, NY 10027, USA.

Annals of the New York Academy of Sciences
|December 14, 2004
PubMed
Summary

Structural insights into carnitine acyltransferases (CrAT) reveal a conserved fold and an active site tunnel. This provides a molecular basis for understanding enzyme catalysis and designing therapeutic inhibitors for metabolic diseases.

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

Author Correction: Quantification and transcriptome profiling reveal abundant, dynamic and translatable dephospho-CoA-capped RNAs.

Nature biotechnology·2026
Same author

Assessing Metal Ion Assignment Accuracy in Protein Data Bank Models via Elemental Spectroscopy.

Journal of chemical information and modeling·2026
Same author

YBX1 takes actions on triggering M2-like polarization of macrophages and stabilizing CXCL8 mRNA to exhibit its metastatic potential in bladder cancer.

International immunopharmacology·2026
Same author

Crystal structure of mouse DXO in complex with the UDP-N-acetylglucosamine cap and molecular mechanism for the decapping reactions.

Nucleic acids research·2026
Same author

Orthosteric and allosteric effects of anti-CRISPR II-C1 inhibition on <i>Geo</i> Cas9 from integrated structural biophysics.

bioRxiv : the preprint server for biology·2026
Same author

A spring-loaded grip-and-pull mechanism for stepwise RNA duplex unwinding by Xrn1.

Nucleic acids research·2026

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Carnitine acyltransferases (CrATs) are vital enzymes involved in acyl group exchange between carnitine and coenzyme A (CoA).
  • Carnitine palmitoyltransferases (CPTs) are critical for mitochondrial fatty acid beta-oxidation, with CPT-I activity regulated by malonyl-CoA.
  • Dysregulation of CrATs is linked to severe human diseases, making them therapeutic targets for type 2 diabetes and obesity.

Purpose of the Study:

  • To determine the crystal structures of murine carnitine acetyltransferase (CrAT).
  • To elucidate the structural basis of CrAT catalysis and substrate binding.
  • To provide insights for the rational design of CrAT inhibitors.

Main Methods:

  • X-ray crystallography was employed to determine the structures of murine CrAT.

Related Experiment Videos

  • Structures were solved for the apoenzyme and in complex with substrates carnitine and CoA.
  • Structural analysis focused on domain organization, active site architecture, and substrate positioning.

    • Main Results:

    • The crystal structures revealed a conserved backbone fold shared between the two domains of CrAT, similar to other transferase enzymes.
    • The active site is located at the interface between the two domains, forming a tunnel where carnitine and CoA bind.
    • Carnitine and CoA bind on opposite sides of the catalytic His343 residue within the active site tunnel.

    Conclusions:

    • The determined structures provide a detailed molecular understanding of carnitine acyltransferase catalysis.
    • The findings offer a structural foundation for developing inhibitors targeting these enzymes.
    • Structural data suggests carnitine may play a role in stabilizing catalytic intermediates.