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

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

14.5K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
14.5K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

5.7K
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...
5.7K
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
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

20.4K
Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
20.4K
Mechanism of Conjugation01:19

Mechanism of Conjugation

1.6K
Bacterial conjugation is a mechanism of horizontal gene transfer that enables the exchange of genetic material between bacterial cells through direct contact. This process is facilitated by a donor cell carrying a conjugative plasmid, which encodes genes necessary for pilus formation, DNA replication, and transfer. The conjugative plasmid plays a central role in initiating and executing the transfer of genetic material.The tra region of the conjugative plasmid encodes proteins responsible for...
1.6K
DNA Topoisomerases02:02

DNA Topoisomerases

38.1K
Topoisomerases are enzymes that relax overwound DNA molecules during various cell processes, including DNA replication and transcription. These enzymes regulate positive and negative DNA supercoiling without changing the nucleotide sequence. DNA overwinding in a clockwise direction results in positively supercoiled DNA, whereas underwinding in a counterclockwise direction produces negatively supercoiled DNA.
Types and Mechanism of action
Topoisomerases are divided into two main types. ...
38.1K

You might also read

Related Articles

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

Sort by
Same author

Hydroxamate-based inhibitors reveal structural determinants of selectivity for Plasmodium falciparum aminopeptidase P.

The Journal of biological chemistry·2026
Same author

Kinetic and structural characterisation of domain-specific angiotensin I-converting enzyme inhibition by captopril, rentiapril and zofenoprilat.

The FEBS journal·2026
Same author

Correction: Molecular basis of acyl-CoA ester recognition by α-methylacyl-CoA racemase from Mycobacterium tuberculosis.

The Journal of biological chemistry·2025
Same author

Structural basis for inhibition of Mycobacterium tuberculosis α-methylacyl-CoA racemase by 2-arylthiopropanoyl-CoA inhibitor analogs.

The Journal of biological chemistry·2025
Same author

Ciprofloxacin Inhibits Angiotensin I‑Converting Enzyme (ACE) Activity by Binding at the Exosite, Distal to the Catalytic Pocket.

ACS bio & med chem Au·2025
Same author

Molecular basis of domain-specific angiotensin I-converting enzyme inhibition by the antihypertensive drugs enalaprilat, ramiprilat, trandolaprilat, quinaprilat and perindoprilat.

The FEBS journal·2025

Related Experiment Video

Updated: Apr 15, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
13:34

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

12.1K

Structure and function of a Clostridium difficile sortase enzyme.

Christopher J Chambers1, April K Roberts2, Clifford C Shone2

  • 11] Public Health England, Porton Down, Salisbury SP4 0JG, UK [2] Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.

Scientific Reports
|March 25, 2015
PubMed
Summary
This summary is machine-generated.

Sortase SrtB anchors proteins to the cell wall in Clostridioides difficile. However, this study found the SrtB enzyme is not essential for pathogenesis in animal models.

More Related Videos

A Purification and In Vitro Activity Assay for a pppGpp Synthetase from Clostridium difficile
09:53

A Purification and In Vitro Activity Assay for a pppGpp Synthetase from Clostridium difficile

Published on: November 3, 2018

9.1K
A Protocol to Characterize the Morphological Changes of Clostridium difficile in Response to Antibiotic Treatment
12:58

A Protocol to Characterize the Morphological Changes of Clostridium difficile in Response to Antibiotic Treatment

Published on: May 25, 2017

9.5K

Related Experiment Videos

Last Updated: Apr 15, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
13:34

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

12.1K
A Purification and In Vitro Activity Assay for a pppGpp Synthetase from Clostridium difficile
09:53

A Purification and In Vitro Activity Assay for a pppGpp Synthetase from Clostridium difficile

Published on: November 3, 2018

9.1K
A Protocol to Characterize the Morphological Changes of Clostridium difficile in Response to Antibiotic Treatment
12:58

A Protocol to Characterize the Morphological Changes of Clostridium difficile in Response to Antibiotic Treatment

Published on: May 25, 2017

9.5K

Area of Science:

  • Microbiology
  • Structural Biology
  • Bacterial Pathogenesis

Background:

  • Sortase enzymes anchor proteins to the cell wall in Gram-positive bacteria.
  • Sortases are crucial for pathogenesis in some bacteria, like Staphylococcus aureus, and are therapeutic targets.

Purpose of the Study:

  • To structurally characterize the Clostridioides difficile sortase.
  • To elucidate the role of C. difficile sortase in cell wall biogenesis and pathogenesis.

Main Methods:

  • X-ray diffraction was used to determine the structure of an active site mutant C. difficile sortase.
  • A C. difficile sortase knockout strain was created using intron mutagenesis.
  • The knockout strain was characterized in an animal model of C. difficile infection.

Main Results:

  • The crystal structure of C. difficile sortase was determined to 2.55 Å, providing insight into its catalytic mechanism.
  • The sortase SrtB was identified as the enzyme anchoring the adhesin CD0386 to the peptidoglycan.
  • An SPKTG peptide motif was found to be involved in the transpeptidation reaction.
  • The SrtB knockout mutant showed a similar disease onset rate as the wild-type strain in an animal model.

Conclusions:

  • The SrtB enzyme from C. difficile does not play an essential role in pathogenesis.
  • Structural and functional characterization of C. difficile sortase provides insights into its mechanism.