Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Ligand Binding and Linkage

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....

Assembly of Signaling Complexes

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

Coupled Reactions

Coupled Reactions

Cellular processes such as building and breaking down complex molecules occur through stepwise chemical reactions. Some of these chemical reactions are spontaneous and release energy, whereas others require energy to proceed. Cells often couple the energy-releasing reaction with the energy-requiring one to carry out important cell functions.
Energy in adenosine triphosphate or ATP molecules is easily accessible to do work. ATP powers the majority of energy-requiring cellular reactions....

You might also read

Related Articles

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

Sort by

Same author

The intrinsically disordered region of the human parathyroid hormone controls functional amyloid properties.

The Journal of biological chemistry·2026

Same author

Total Synthesis and Structural Revision of Keenamide A.

Journal of natural products·2026

Same author

Mechanism of SHP2 activation by bis-Tyr-phosphorylated Gab1.

Structure (London, England : 1993)·2025

Same author

Strategies for mitigating radiation damage and improving data completeness in 3D electron diffraction of protein crystals.

Acta crystallographica. Section D, Structural biology·2025

Same author

Preparing submicrometer crystals for electron diffraction.

Nature protocols·2024

Same author

Delineating organizational principles of the endogenous L-A virus by cryo-EM and computational analysis of native cell extracts.

Communications biology·2024

Search research articles

Related Experiment Video

Updated: Jul 23, 2025

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

Coupling proteins, with deadly consequences.

Jochen Balbach^1,2, Milton T Stubbs^2,3

¹Institut für Physik, Martin-Luther-Universität Halle-Wittenberg, Halle (Saale), Germany.

Science (New York, N.Y.)

|July 13, 2023

Summary

This summary is machine-generated.

Bacteriophage protein E inhibits bacterial cell wall synthesis, leading to bacterial death. This mechanism offers a novel approach for developing new antibacterial strategies.

More Related Videos

A Data Integration Workflow to Identify Drug Combinations Targeting Synthetic Lethal Interactions

A Data Integration Workflow to Identify Drug Combinations Targeting Synthetic Lethal Interactions

Published on: May 27, 2021

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Related Experiment Videos

Last Updated: Jul 23, 2025

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

A Data Integration Workflow to Identify Drug Combinations Targeting Synthetic Lethal Interactions

A Data Integration Workflow to Identify Drug Combinations Targeting Synthetic Lethal Interactions

Published on: May 27, 2021

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Area of Science:

Bacteriology
Molecular Biology
Biochemistry

Background:

Bacterial cell wall biosynthesis is essential for bacterial survival.
Bacteriophages are viruses that infect bacteria and have potential as therapeutic agents.
Understanding phage-host interactions is crucial for developing novel antibacterial strategies.

Purpose of the Study:

To investigate the mechanism by which bacteriophage protein E kills bacteria.
To elucidate the role of protein E in inhibiting bacterial cell wall biosynthesis.

Main Methods:

Bacterial culture and viability assays.
Enzyme activity assays for cell wall biosynthesis pathways.
Protein expression and purification.

Main Results:

Phage protein E was identified as the key factor responsible for bacterial lysis.
Protein E directly inhibits enzymes involved in peptidoglycan synthesis.
Inhibition of cell wall biosynthesis leads to rapid bacterial cell death.

Conclusions:

Bacteriophage protein E represents a potent antibacterial agent by targeting essential cell wall synthesis pathways.
This finding opens new avenues for phage-derived antibacterial therapies.