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

You might also read

Related Articles

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

Sort by
Same author

Nontraditional Roles of Magnesium Ions in Modulating Sav2152: Insight from a Haloacid Dehalogenase-like Superfamily Phosphatase from <i>Staphylococcus aureus</i>.

International journal of molecular sciences·2024
Same author

Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases.

Life (Basel, Switzerland)·2021
Same author

Molecular Interactions between Two LMP2A PY Motifs of EBV and WW Domains of E3 Ubiquitin Ligase AIP4.

Life (Basel, Switzerland)·2021
Same author

Rational discovery of antimetastatic agents targeting the intrinsically disordered region of MBD2.

Science advances·2019
Same author

Structural hierarchy controlling dimerization and target DNA recognition in the AHR transcriptional complex.

Proceedings of the National Academy of Sciences of the United States of America·2017

Related Experiment Video

Updated: Jul 31, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.0K

Crystal structure of the engineered endolysin mtEC340M.

Jee Min Wang1, Seung Hyeon Seok2, Won Su Yoon1

  • 1Department of Molecular Science and Technology, Ajou University, Suwon, Gyeonggi 16499, Republic of Korea.

Acta Crystallographica. Section F, Structural Biology Communications
|May 3, 2023
PubMed
Summary

Engineered endolysins show promise as antibacterial agents. Structural analysis of mtEC340M reveals its potential for combating antibiotic-resistant bacteria by targeting cell walls.

Keywords:
Gram-negative bacteriaantibacterial agentscrystal structureendolysin mtEC340Mendolysins

More Related Videos

From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

13.5K
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

11.6K

Related Experiment Videos

Last Updated: Jul 31, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.0K
From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

13.5K
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

11.6K

Area of Science:

  • Microbiology and Structural Biology
  • Bacteriophage research
  • Antibiotic resistance mechanisms

Background:

  • Bacteriophage endolysins degrade bacterial peptidoglycan for phage release.
  • Endolysins are a novel class of antibacterial agents against antibiotic-resistant bacteria.
  • The PBEC131 phage infects Escherichia coli.

Purpose of the Study:

  • To determine the crystal structure of the engineered endolysin mtEC340M.
  • To understand the structural basis for the antibacterial activity of mtEC340M.
  • To identify potential active residues for therapeutic applications.

Main Methods:

  • X-ray crystallography was used to determine the crystal structure of mtEC340M.
  • The structure was resolved at a resolution of 2.4 Å.
  • Structural comparison with known peptidoglycan-degrading lysozymes was performed to predict active residues.

Main Results:

  • The crystal structure of mtEC340M was determined, revealing a fold comprising eight α-helices and two loops.
  • The three-dimensional structure provides insights into the enzyme's architecture.
  • Structural comparison allowed for the prediction of three active residues crucial for enzymatic function.

Conclusions:

  • The determined crystal structure of mtEC340M offers a foundation for understanding its antibacterial mechanism.
  • This structural information can guide the development of novel endolysin-based antibacterial therapies.
  • Engineered endolysins like mtEC340M represent a promising strategy to combat the growing threat of antibiotic resistance.