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

3.9K
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...
3.9K
Protein Modifications in the RER01:26

Protein Modifications in the RER

7.7K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
7.7K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

5.8K
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...
5.8K
Protein Glycosylation01:25

Protein Glycosylation

10.8K
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...
10.8K
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

8.1K
Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
8.1K
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

3.7K
The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
3.7K

You might also read

Related Articles

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

Sort by
Same author

Assessing <i>Corynebacterium glutamicum</i> as a surrogate of <i>Mycobacterium tuberculosis</i> for DNA gyrase inhibitor design.

bioRxiv : the preprint server for biology·2026
Same author

Functional dissection of <i>Corynebacterium glutamicum</i> Wag31 domains for septal recruitment and polar distribution during the cell cycle.

mBio·2026
Same author

Molecular mechanisms of transhydrogenase activity and allosteric regulation in eukaryotic type II PHGDH Ser33.

Nature communications·2026
Same author

Essential role of MptB in the biosynthesis of phosphatidylinositol mannosides, lipomannan and lipoarabinomannan in mycobacteria.

The Journal of biological chemistry·2026
Same author

Structural basis for phosphorylation and allosteric regulation of bacterial glycogen phosphorylase by histidine phosphocarrier protein.

Nature communications·2026
Same author

Monoclonal antibodies against nitrated nerve growth factor reveal an oxidation-dependent pathogenic hallmark in ALS.

Proceedings of the National Academy of Sciences of the United States of America·2026

Related Experiment Video

Updated: Apr 20, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

7.2K

Secondary structure reshuffling modulates glycosyltransferase function at the membrane.

David Giganti1, David Albesa-Jové2, Saioa Urresti2

  • 11] Institut Pasteur, Unité de Microbiologie Structurale, CNRS UMR 3528, Paris, France. [2] Unidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Cientificas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Leioa, Bizkaia, Spain. [3] Departamento de Bioquímica, Universidad del País Vasco, Spain.

Nature Chemical Biology
|November 18, 2014
PubMed
Summary

Protein refolding is crucial for cellular function. Mannosyltransferase PimA exhibits remarkable flexibility, undergoing structural changes that modulate its catalytic activity, especially when interacting with membrane phospholipids.

More Related Videos

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

2.8K
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

13.3K

Related Experiment Videos

Last Updated: Apr 20, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

7.2K
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

2.8K
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

13.3K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Protein secondary structure refolding is essential for biological processes, influencing protein conformation and function.
  • Mannosyltransferase PimA is involved in cellular pathways, and its structural dynamics are critical for its activity.

Purpose of the Study:

  • To investigate the structural flexibility of mannosyltransferase PimA during its catalytic cycle.
  • To understand how structural transitions in PimA modulate its catalytic function.
  • To elucidate the role of anionic phospholipids in promoting these structural changes.

Main Methods:

  • X-ray crystallography was employed to determine the crystal structures of mannosyltransferase PimA.
  • Analysis of structural data to identify conformational changes throughout the catalytic cycle.

Main Results:

  • The crystal structures reveal exceptional flexibility in mannosyltransferase PimA.
  • Key structural transitions, including β-strand-to-α-helix and α-helix-to-β-strand, were observed.
  • These conformational changes are linked to the modulation of catalysis.

Conclusions:

  • Mannosyltransferase PimA undergoes significant structural refolding during catalysis.
  • Interactions with anionic phospholipids in the membrane promote these dynamic structural changes.
  • The flexibility of PimA is a key determinant of its catalytic efficiency and regulation.