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Conserved binding mode but diverse interfaces of MreC-PBP2 interactions
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DOI：10.1002/1873-3468.70409.png)
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Abstract
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MreC is an essential periplasmic component of the bacterial elongasome that regulates peptidoglycan synthesis through interaction with PBP2. Here, we report the crystal structure of MreC from Acinetobacter baumannii (abMreC) at 2.49 Å resolution. The structure reveals a conserved elongated fold composed of two β-barrel domains and exists as a monomer in solution. Structural comparison with homologs shows that while the overall architecture is conserved, surface-exposed regions involved in protein–protein interactions vary significantly. AlphaFold3-based modeling of the abMreC–abPBP2 complex, supported by mutational and pull-down assays, identifies key interface residues. Comparison with the Helicobacter pylori complex indicates that MreC employs a conserved binding mode while accommodating diverse interface architectures to regulate PBP2 activity.
Keywords:
Acinetobacter baumannii
Crystal structure
MreC
Penicillin
Superbug
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