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Conserved binding mode but diverse interfaces of MreC-PBP2 interactions
Hyunseok Jang1,2, Hyo Been Jin1,2, Chang Min Kim3
1College of Pharmacy, Chung-Ang University, Seoul, Republic of Korea.
FEBS Letters
|July 9, 2026
Summary
The bacterial cell wall protein MreC, essential for peptidoglycan synthesis, was structurally characterized in Acinetobacter baumannii. Its interaction with PBP2 reveals conserved binding modes despite variable interfaces, crucial for bacterial shape and survival.
Area of Science:
- Bacterial cell wall biogenesis
- Structural biology
- Protein-protein interactions
Background:
- MreC is a key component of the bacterial elongasome, a complex responsible for cell shape and division.
- It regulates peptidoglycan synthesis by interacting with penicillin-binding protein 2 (PBP2).
- Understanding MreC structure and interactions is vital for deciphering bacterial cell envelope construction.
Purpose of the Study:
- To determine the crystal structure of MreC from Acinetobacter baumannii (abMreC).
- To investigate the structural basis of abMreC interaction with abPBP2.
- To compare the binding mode of MreC across different bacterial species.
Main Methods:
- X-ray crystallography for abMreC structure determination.
- AlphaFold3-based computational modeling for abMreC-abPBP2 complex prediction.
- In vitro mutational and pull-down assays to validate protein interactions.
Main Results:
- The crystal structure of abMreC was resolved at 2.49 Å, revealing a conserved two β-barrel domain fold.
- abMreC functions as a monomer in solution.
- Structural analysis and computational modeling identified key residues at the abMreC-abPBP2 interface.
- Surface regions involved in protein interactions showed significant variability among homologs.
Conclusions:
- A. baumannii MreC shares a conserved fold with homologs but exhibits distinct surface features for interaction.
- MreC utilizes a conserved binding mechanism to regulate PBP2 activity, adapting to varied interface architectures.
- This study provides structural insights into bacterial elongasome function and potential targets for antimicrobial development.
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