9c3f | pdb_00009c3f

Cryo-EM structure of E. coli AmpG

spinqualitylabelsall models 9c3f, resolution 3.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9c3f is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.78Å Ligands: LMT, PEE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C562_ECOLX Electron-transport protein of unknown function.AMPG_ECOLI Permease involved in cell wall peptidoglycan recycling (PubMed:12426329, PubMed:8878601). Transports, from the periplasm into the cytoplasm, the disaccharide N-acetylglucosaminyl-beta-1,4-anhydro-N-acetylmuramic acid (GlcNAc-anhMurNAc) and GlcNAc-anhMurNAc-peptides (PubMed:12426329). Transport is dependent on the proton motive force (PubMed:12426329). AmpG is also involved in beta-lactamase induction (PubMed:7773404). Publication Abstract from PubMed 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 beta-lactam antibiotic induced cell wall damage. In some species, these products upregulate the beta-lactamase AmpC, which hydrolyzes beta-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. Cryo-EM characterization of the anydromuropeptide permease AmpG central to bacterial fitness and beta-lactam antibiotic resistance.,Sverak HE, Yaeger LN, Worrall LJ, Vacariu CM, Glenwright AJ, Vuckovic M, Al Azawi ZD, Lamers RP, Marko VA, Skorupski C, Soni AS, Tanner ME, Burrows LL, Strynadka NC Nat Commun. 2024 Nov 16;15(1):9936. doi: 10.1038/s41467-024-54219-9. PMID:39548104 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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