9C3F
Cryo-EM structure of E. coli AmpG
Summary for 9C3F
| Entry DOI | 10.2210/pdb9c3f/pdb |
| EMDB information | 45167 |
| Descriptor | Anhydromuropeptide permease,Soluble cytochrome b562, DODECYL-BETA-D-MALTOSIDE, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (3 entities in total) |
| Functional Keywords | membrane protein, major facilitator family transporter, cell wall, antibiotic resistance |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 1 |
| Total formula weight | 66581.88 |
| Authors | |
| Primary citation | Sverak, H.E.,Yaeger, L.N.,Worrall, L.J.,Vacariu, C.M.,Glenwright, A.J.,Vuckovic, M.,Al Azawi, Z.D.,Lamers, R.P.,Marko, V.A.,Skorupski, C.,Soni, A.S.,Tanner, M.E.,Burrows, L.L.,Strynadka, N.C. Cryo-EM characterization of the anydromuropeptide permease AmpG central to bacterial fitness and beta-lactam antibiotic resistance. Nat Commun, 15:9936-9936, 2024 Cited by PubMed Abstract: Bacteria invest significant resources into the continuous creation and tailoring of their essential protective peptidoglycan (PG) cell wall. Several soluble PG biosynthesis products in the periplasm are transported to the cytosol for recycling, leading to enhanced bacterial fitness. GlcNAc-1,6-anhydroMurNAc and peptide variants are transported by the essential major facilitator superfamily importer AmpG in Gram-negative pathogens including Escherichia coli, Klebsiella pneumoniae, Acinetobacter baumannii, and Pseudomonas aeruginosa. Accumulation of GlcNAc-1,6-anhydroMurNAc-pentapeptides also results from β-lactam antibiotic induced cell wall damage. In some species, these products upregulate the β-lactamase AmpC, which hydrolyzes β-lactams to allow for bacterial survival and drug-resistant infections. Here, we have used cryo-electron microscopy and chemical synthesis of substrates in an integrated structural, biochemical, and cellular analysis of AmpG. We show how AmpG accommodates the large GlcNAc-1,6-anhydroMurNAc peptides, including a unique hydrophobic vestibule to the substrate binding cavity, and characterize residues involved in binding that inform the mechanism of proton-mediated transport. PubMed: 39548104DOI: 10.1038/s41467-024-54219-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.78 Å) |
Structure validation
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