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Structural and functional insights of AmpG in muropeptide transport and multiple β-lactam antibiotics resistance
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Structural and functional insights of AmpG in muropeptide transport and multiple β-lactam antibiotics resistance
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Journal Article
Structural and functional insights of AmpG in muropeptide transport and multiple β-lactam antibiotics resistance
2025
Overview
Anhydromuropeptide permease (AmpG) is a transporter protein located in the inner membrane of certain gram -negative bacteria, involved in peptidoglycan (PG) recycling and β-lactamase induction. Decreased AmpG function reduces resistance of antibiotic-resistant bacteria to β-lactam antibiotics. Therefore, AmpG-targeting inhibitors are promising ‘antibiotic adjuvants’. However, as the tertiary structure of AmpG has not yet been identified, the development of targeted inhibitors remains challenging. We present four cryo-electron microscopy (cryo-EM) structures: the apo-inward and apo-outward state structures and the inward-occluded and outward states complexed with the substrate GlcNAc-1,6-anhMurNAc. Through functional analysis and molecular dynamics (MD) simulations, we identified motif A, which stabilizes the outward state, substrate-binding pocket, and protonation-related residues. Based on the structure of AmpG and our experimental results, we propose a muropeptide transport mechanism for AmpG. A deeper understanding of its structure and transport mechanism provides a foundation for the development of antibiotic adjuvants.
Here, the authors present cryo-EM structures of Anhydromuropeptide permease in apo-inward, apo-outward, inward-occluded, and an outward-facing substrate, providing mechanistic insights into muropeptide translocation.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/80
/ Amides
/ Anti-Bacterial Agents - pharmacology
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Drug Resistance, Multiple, Bacterial
/ Escherichia coli - drug effects
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Humanities and Social Sciences
/ Membrane Transport Proteins - chemistry
/ Membrane Transport Proteins - genetics
/ Membrane Transport Proteins - metabolism
/ Membrane Transport Proteins - ultrastructure
/ Molecular Dynamics Simulation
/ Mutation
/ Peptides
/ Permease
/ Science
