9J9Z
Cryo-EM structure of Outward state Anhydromuropeptide permease (AmpG) complex with GlcNAc-1,6-anhMurNAc
Summary for 9J9Z
| Entry DOI | 10.2210/pdb9j9z/pdb |
| EMDB information | 61285 |
| Descriptor | anti-BRIL Fab Heavy chain, anti-BRIL Fab Nanobody, anti-BRIL Fab Light chain, ... (5 entities in total) |
| Functional Keywords | ampg, mfs, anhydromuropeptide permease, membrane protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 4 |
| Total formula weight | 125473.34 |
| Authors | |
| Primary citation | Chang, N.,Kim, H.,Kim, U.,Cho, Y.,Yoo, Y.,Lee, H.,Kim, J.W.,Kim, M.S.,Lee, J.,Cho, Y.L.,Kim, K.,Yong, D.,Cho, H.S. Structural and functional insights of AmpG in muropeptide transport and multiple beta-lactam antibiotics resistance. Nat Commun, 16:5744-5744, 2025 Cited by PubMed Abstract: 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. PubMed: 40593790DOI: 10.1038/s41467-025-61169-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.97 Å) |
Structure validation
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