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

2.9K
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...
2.9K
Protein Glycosylation01:25

Protein Glycosylation

7.1K
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...
7.1K
Structural Protein Function01:56

Structural Protein Function

2.8K
2.8K
Structure of Cadherins01:25

Structure of Cadherins

3.4K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
3.4K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.8K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.8K
Proteoglycans01:05

Proteoglycans

4.0K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
4.0K

You might also read

Related Articles

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

Sort by
Same author

Structures of ALG3/9/12 reveal the assembly logic of the N-glycan oligomannose core.

Nature chemical biology·2026
Same author

GLYCO-BUILD: an enzymatic pipeline for the synthesis of peptides carrying eukaryotic N-glycans.

Nature communications·2025
Same author

Doxorubicin Recognition and Transport by the MATE Multidrug Transporter NorM From Vibrio cholerae.

Journal of molecular biology·2025
Same author

Corrigendum to "Structural Basis of Drug Recognition by the Multidrug Transporter ABCG2". [J. Mol. Biol. 433 (2021) 166980].

Journal of molecular biology·2025
Same author

Structural basis of drug recognition by human MATE1 transporter.

Nature communications·2025
Same author

Structure of nanobody-inhibited state of human bile salt transporter NTCP.

Structure (London, England : 1993)·2025

Related Experiment Video

Updated: Aug 9, 2025

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
13:35

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota

Published on: May 23, 2025

538

Emerging structural insights into C-type glycosyltransferases.

J Andrew N Alexander1, Kaspar P Locher1

  • 1Institute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland.

Current Opinion in Structural Biology
|February 24, 2023
PubMed
Summary

Glycosyltransferases of the C superfamily (GT-Cs) are crucial enzymes. Recent structural studies reveal novel folds and two subclasses, GT-CA and GT-CB, expanding our understanding of these essential biological catalysts.

More Related Videos

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition
07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.4K
Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
12:29

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility

Published on: March 11, 2022

2.3K

Related Experiment Videos

Last Updated: Aug 9, 2025

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
13:35

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota

Published on: May 23, 2025

538
Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition
07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.4K
Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
12:29

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility

Published on: March 11, 2022

2.3K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Glycosyltransferases of the C superfamily (GT-Cs) are ubiquitous enzymes essential for synthesizing complex carbohydrates.
  • GT-Cs mediate critical glycosylation processes, including C-, N-, and O-linked modifications, vital for eukaryotic protein function.
  • Previously, GT-Cs were characterized by a conserved 7-transmembrane helix structural module.

Purpose of the Study:

  • To analyze the structural diversity within the GT-C superfamily.
  • To identify and discuss the emergence of distinct subclasses within GT-Cs.
  • To highlight the need for further structural studies to understand GT-C function.

Main Methods:

  • Bioinformatic analysis of GT-C sequences and structures.
  • Comparative structural analysis of known GT-C proteins.
  • Literature review of recent GT-C structural discoveries.

Main Results:

  • Recent structural data reveal novel and diverse folds within the GT-C superfamily, challenging the 7-transmembrane helix model.
  • Two distinct subclasses, GT-CA and GT-CB, have emerged based on structural and potentially functional divergence.
  • The growing diversity underscores the complexity of GT-C evolution and function.

Conclusions:

  • The GT-C superfamily exhibits greater structural diversity than previously recognized.
  • The identification of GT-CA and GT-CB subclasses provides a framework for future research.
  • Elucidating substrate-bound structures is crucial for a molecular understanding of glycan recognition and catalysis in these subclasses.