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 Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
tRNA Activation02:26

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Conservatives Belong in Public Health.

American journal of public health·2026
Same author

Functional Analysis of the Halastavi árva Virus (HalV) Internal Ribosome Entry Site.

Viruses·2026
Same author

Drugging the intrinsically disordered transactivation domain of androgen receptor.

Signal transduction and targeted therapy·2026
Same author

ZW191, an FRα-Targeted Topoisomerase 1 Inhibitor ADC with a Differentiated Antitumor Efficacy and Tolerability Profile.

Clinical cancer research : an official journal of the American Association for Cancer Research·2026
Same author

Does osteogenesis imperfecta predispose infants to metaphyseal fractures? A systematic review.

BMJ paediatrics open·2026
Same author

Systematic Evaluation of Maleimide Spacer Impact on Drug-Linker Deconjugation in Antibody-Drug Conjugates <i>Ex Vivo</i> and <i>In Vivo</i>.

Bioconjugate chemistry·2026

Related Experiment Video

Updated: Jun 19, 2026

Generation of Monocyte-Derived Dendritic Cells with Differing Sialylated Phenotypes
13:36

Generation of Monocyte-Derived Dendritic Cells with Differing Sialylated Phenotypes

Published on: October 20, 2023

Structural insight into mammalian sialyltransferases.

Francesco V Rao1, Jamie R Rich, Bojana Rakić

  • 1Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada.

Nature Structural & Molecular Biology
|October 13, 2009
PubMed
Summary

The crystal structure of a mammalian sialyltransferase (ST) enzyme was determined. This provides a structural basis for understanding ST mechanisms and designing targeted inhibitors for cell surface modification.

More Related Videos

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy
08:16

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy

Published on: February 7, 2025

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

Related Experiment Videos

Last Updated: Jun 19, 2026

Generation of Monocyte-Derived Dendritic Cells with Differing Sialylated Phenotypes
13:36

Generation of Monocyte-Derived Dendritic Cells with Differing Sialylated Phenotypes

Published on: October 20, 2023

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy
08:16

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy

Published on: February 7, 2025

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Glycobiology

Background:

  • Mammalian cell surfaces feature complex glycoconjugates crucial for cell recognition and immunity.
  • Sialic acid-terminated glycans play vital roles in cellular processes.
  • Sialyltransferases (STs) are enzymes responsible for adding sialic acid to glycoconjugates.

Purpose of the Study:

  • To elucidate the structural basis of mammalian sialyltransferase function.
  • To provide insights into the mechanism and specificity of ST enzymes.
  • To facilitate the rational design of selective ST inhibitors.

Main Methods:

  • X-ray crystallography was employed to determine the 3D structure.
  • The study focused on a specific mammalian enzyme, porcine ST3Gal-I.

Main Results:

  • The crystal structure of porcine ST3Gal-I, a mammalian sialyltransferase, was successfully determined.
  • This structure offers a detailed view of the enzyme's active site and overall architecture.
  • The findings provide a foundation for understanding how STs recognize their substrates and catalyze sialylation.

Conclusions:

  • The presented crystal structure of porcine ST3Gal-I offers a significant structural foundation.
  • Understanding ST structure is key to deciphering sialylation mechanisms and enzyme specificity.
  • This knowledge is crucial for developing targeted inhibitors for therapeutic applications.