9C3F

Cryo-EM structure of E. coli AmpG

9C3F の概要

• エントリーDOI: 10.2210/pdb9c3f/pdb
• EMDBエントリー: 45167
• 分子名称: Anhydromuropeptide permease,Soluble cytochrome b562, DODECYL-BETA-D-MALTOSIDE, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (3 entities in total)
• 機能のキーワード: membrane protein, major facilitator family transporter, cell wall, antibiotic resistance
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 66581.88

構造登録者

Sverak, H.,Worrall, L.J.,Strynadka, N.C.J. (登録日: 2024-05-31, 公開日: 2024-12-18, 最終更新日: 2025-06-04)

主引用文献

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

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: 39548104
DOI: 10.1038/s41467-024-54219-9

実験手法

ELECTRON MICROSCOPY (3.78 Å)