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Related Experiment Video

Updated: Jun 7, 2025

Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions

Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions

Published on: October 13, 2015

Structural and Functional Insight Into YefM-YoeB Complex of Toxin-Antitoxin System From Streptococcus pneumoniae.

Do-Hee Kim¹, Yong-Chan Lee², Chenglong Jin^2,3

¹Research Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Seoul, Republic of Korea.

Journal of Cellular Biochemistry

|November 12, 2024

Summary

This summary is machine-generated.

The YefM-YoeB toxin-antitoxin system in Streptococcus pneumoniae was structurally and functionally characterized. Understanding this system offers potential for developing new antibiotics against drug-resistant bacterial infections.

Keywords:

Streptococcus pneumoniae X‐ray crystallography YefM–YoeB antibiotics toxin–antitoxin system

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Last Updated: Jun 7, 2025

Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions

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Published on: October 13, 2015

Producing Gene Deletions in Escherichia coli by P1 Transduction with Excisable Antibiotic Resistance Cassettes

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Quantifying Yersinia pseudotuberculosis Type III Secretion System Activity Following Iron Starvation and Anaerobic Growth

Quantifying Yersinia pseudotuberculosis Type III Secretion System Activity Following Iron Starvation and Anaerobic Growth

Published on: May 31, 2024

Area of Science:

Microbiology
Structural Biology
Molecular Biology

Background:

Streptococcus pneumoniae causes severe diseases like pneumonia and meningitis.
Antibiotic resistance necessitates novel therapeutic mechanisms.
Toxin-antitoxin (TA) systems, like YefM-YoeB, are potential antimicrobial targets.

Purpose of the Study:

To elucidate the structural basis of the YefM-YoeB TA system in S. pneumoniae.
To investigate the functional activity of the YoeB toxin.
To understand the binding interactions for potential drug development.

Main Methods:

X-ray crystallography to determine the YefM-YoeB complex structure.
In vitro ribonuclease activity assays for YoeB toxin.
Analytical ultracentrifugation to determine the oligomeric state in solution.

Main Results:

The crystal structure of the S. pneumoniae YefM-YoeB complex was determined.
The ribonuclease activity of the YoeB toxin was confirmed.
The oligomeric state and a proposed DNA-binding mode of the complex were investigated.

Conclusions:

Structural and functional data provide insights into TA system mechanisms.
The YefM-YoeB system is a promising target for novel antibiotic development.
Targeting this system could combat antibiotic-resistant S. pneumoniae infections.