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

Bacterial Toxins01:12

Bacterial Toxins

43
Bacterial toxins are sophisticated virulence factors that enable pathogenic bacteria to interact with, invade, and damage host tissues. These toxins fall broadly into two types: protein exotoxins, which are secreted into the environment and target specific host receptors, and lipopolysaccharide endotoxins, which are structural components of the bacterial outer membrane released primarily during bacterial lysis or membrane shedding. Exotoxins generally act more selectively, binding to cell...
43

You might also read

Related Articles

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

Sort by
Same author

<sup>64</sup>Cu Hypoxia Imaging Radiotracer Targeting the Human Copper Transporter.

Neuromolecular medicine·2026
Same author

hexABC seeking the physical code of DNA.

Nature communications·2026
Same author

Glutamine Tautomerization Drives RhoGAP-Aided GTP Hydrolysis in Small Rho GTPases.

Journal of the American Chemical Society·2026
Same author

Decoding Cancer-Associated Mutations in DNA Polymerase η through Atomistic Simulations.

Journal of chemical theory and computation·2026
Same author

U2 snRNP recognizes the branch site through a loaded-spring strand-invasion mechanism.

Nucleic acids research·2026
Same author

Structural flexibility of the human vault particle revealed by high-resolution cryo-EM and molecular dynamics simulations.

Nature communications·2026

Related Experiment Video

Updated: Mar 29, 2026

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

10.0K

Anthrax Lethal Factor Investigated by Molecular Simulations.

Rolando Hong1, Alessandra Magistrato1, Paolo Carloni1

  • 1International School for Advanced Studies (SISSA/ISAS), CNR-INFM-Democritos National Simulation Center, and Italian Institute of Technology (IIT), Trieste, Italy.

Journal of Chemical Theory and Computation
|December 2, 2015
PubMed
Summary

Computational methods reveal key insights into anthrax lethal factor (LF), a Zn-based enzyme. The study elucidates the Michaelis complex structure, crucial for understanding anthrax toxin's mechanism of action.

More Related Videos

Deciphering the Molecular Mechanism and Function of Pore-Forming Toxins Using Leishmania major
08:17

Deciphering the Molecular Mechanism and Function of Pore-Forming Toxins Using Leishmania major

Published on: October 28, 2022

2.0K
Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
05:56

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

1.9K

Related Experiment Videos

Last Updated: Mar 29, 2026

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

10.0K
Deciphering the Molecular Mechanism and Function of Pore-Forming Toxins Using Leishmania major
08:17

Deciphering the Molecular Mechanism and Function of Pore-Forming Toxins Using Leishmania major

Published on: October 28, 2022

2.0K
Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
05:56

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

1.9K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Chemistry

Background:

  • Anthrax disease is caused by Bacillus anthracis lethal toxin.
  • Anthrax Lethal Factor (LF) is a Zn-based hydrolase within the toxin.
  • Understanding LF's enzymatic mechanism is critical for therapeutic development.

Purpose of the Study:

  • To investigate the structure of the LF Michaelis complex with a MAPKK-like substrate.
  • To elucidate the role of metal binding site interactions and substrate binding in LF's catalytic activity.
  • To explore conformational changes in LF relevant to its function.

Main Methods:

  • Density Functional Theory (DFT) calculations.
  • Molecular Dynamics (MD) simulations.
  • Coarse-grained (CG) modeling techniques.

Main Results:

  • Second-shell ligands significantly influence the metal binding site's structure, energetics, and protonation state.
  • A Zn-bound water molecule acts as the nucleophile in substrate hydrolysis.
  • Substrate binding is primarily mediated by van der Waals interactions.
  • Hydrolyzed bonds exhibit mild polarization by the protein scaffold.
  • Helix α19 adopts a coiled conformation, differing from some crystal structures.

Conclusions:

  • The study provides a detailed computational model of the LF Michaelis complex.
  • Key catalytic residues and interactions governing LF activity have been identified.
  • Findings offer insights into the structural dynamics of LF and potential targets for inhibition.