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

Oxidation of Alkenes: Syn Dihydroxylation with Potassium Permanganate02:21

Oxidation of Alkenes: Syn Dihydroxylation with Potassium Permanganate

Alkenes can be dihydroxylated using potassium permanganate. The method encompasses the reaction of an alkene with a cold, dilute solution of potassium permanganate under basic conditions to form a cis-diol along with a brown precipitate of manganese dioxide.
Pyruvate Oxidation01:15

Pyruvate Oxidation

After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
Oxidation of Alcohols02:37

Oxidation of Alcohols

In this lesson, the oxidation of alcohols is discussed in depth. The various reagents used for oxidation of primary and secondary alcohols are detailed, and their mechanism of action is provided.
The process of oxidation in a chemical reaction is observed in any of the three forms:
Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide02:44

Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide

Alkenes are converted to 1,2-diols or glycols through a process called dihydroxylation. It involves the addition of two hydroxyl groups across the double bond with two different stereochemical approaches, namely anti and syn. Dihydroxylation using osmium tetroxide progresses with syn stereochemistry.
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

You might also read

Related Articles

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

Sort by
Same author

Cryo-electron microscopy of mucins.

Methods in enzymology·2026
Same author

Young secretory proteins go through a phase.

Nature cell biology·2025
Same author

Protein Target Highlights in CASP16: Insights From the Structure Providers.

Proteins·2025
Same author

Simultaneous Binding of Cu<sup>+</sup> and Cu<sup>2+</sup> at the Two-Tiered Copper Binding Site of the Intestinal Mucin MUC2.

Inorganic chemistry·2025
Same author

MUC5AC filaments illuminate the structural diversification of respiratory and intestinal mucins.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

VWD domain stabilization by autocatalytic Asp-Pro cleavage.

Protein science : a publication of the Protein Society·2024

Related Experiment Video

Updated: Jun 21, 2026

Making Conjugation-induced Fluorescent PEGylated Virus-like Particles by Dibromomaleimide-disulfide Chemistry
10:18

Making Conjugation-induced Fluorescent PEGylated Virus-like Particles by Dibromomaleimide-disulfide Chemistry

Published on: May 27, 2018

Dimer interface migration in a viral sulfhydryl oxidase.

Motti Hakim1, Deborah Fass

  • 1Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.

Journal of Molecular Biology
|July 7, 2009
PubMed
Summary
This summary is machine-generated.

African swine fever virus (ASFV) sulfhydryl oxidase pB119L exhibits unique self-assembly, differing from related viral and eukaryotic enzymes. This discovery highlights viral adaptability in protein structure and function.

More Related Videos

A Facile and Efficient Approach for the Production of Reversible Disulfide Cross-linked Micelles
09:57

A Facile and Efficient Approach for the Production of Reversible Disulfide Cross-linked Micelles

Published on: December 23, 2016

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

Related Experiment Videos

Last Updated: Jun 21, 2026

Making Conjugation-induced Fluorescent PEGylated Virus-like Particles by Dibromomaleimide-disulfide Chemistry
10:18

Making Conjugation-induced Fluorescent PEGylated Virus-like Particles by Dibromomaleimide-disulfide Chemistry

Published on: May 27, 2018

A Facile and Efficient Approach for the Production of Reversible Disulfide Cross-linked Micelles
09:57

A Facile and Efficient Approach for the Production of Reversible Disulfide Cross-linked Micelles

Published on: December 23, 2016

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Large double-stranded DNA viruses produce viral proteins in the cytosol, requiring enzymes for disulfide bond formation.
  • Sulfhydryl oxidases, characterized by a Cys-X-X-Cys motif and FAD cofactor, catalyze these oxidative protein folding reactions.
  • Viral sulfhydryl oxidases are typically dimeric with a conserved five-helix fold.

Purpose of the Study:

  • To investigate the self-assembly mechanism of the African swine fever virus (ASFV) sulfhydryl oxidase pB119L.
  • To compare the dimerization interface of ASFV pB119L with homologous enzymes from other viruses and eukaryotes.
  • To explore the evolutionary potential of large DNA viruses in protein structure innovation.

Main Methods:

  • Structural analysis of ASFV pB119L to determine its oligomeric state and quaternary structure.
  • Comparative analysis of protein-protein interaction surfaces between ASFV pB119L and other sulfhydryl oxidases.
  • Bioinformatic analysis to assess the conservation of self-assembly modes across viral sulfhydryl oxidases.

Main Results:

  • ASFV pB119L utilizes a distinct self-assembly interface for dimerization compared to mammalian, plant, and fungal homologs.
  • This alternate dimerization mode is not universal among viral sulfhydryl oxidases, as evidenced by a mimivirus enzyme adopting a eukaryotic-like structure.
  • The findings reveal significant diversity in protein quaternary structure within the viral sulfhydryl oxidase family.

Conclusions:

  • ASFV pB119L showcases a novel protein self-assembly strategy, distinct from known viral and eukaryotic sulfhydryl oxidases.
  • Large DNA viruses can pioneer unique protein structures and assembly mechanisms due to rapid mutation rates and gene acquisition.
  • This study underscores the evolutionary innovation capacity of viruses in protein folding and function.