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TitleStructural and functional insights of AmpG in muropeptide transport and multiple β-lactam antibiotics resistance.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 5744, Year 2025
Publish dateJul 1, 2025
AuthorsNienping Chang / Hoyoung Kim / Uijin Kim / Yongju Cho / Youngki Yoo / Hyunsook Lee / Ji Won Kim / Min Sung Kim / Jaeho Lee / Young-Lag Cho / Kitae Kim / Dongeun Yong / Hyun-Soo Cho /
PubMed AbstractAnhydromuropeptide 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. ...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.
External linksNat Commun / PubMed:40593790 / PubMed Central
MethodsEM (single particle)
Resolution2.97 - 3.88 Å
Structure data

39900

8zbb

EMDB-39900, PDB-8zbb:
Cryo-EM structure of outward state Anhydromuropeptide permease (AmpG) G50W/L269W
Method: EM (single particle) / Resolution: 3.11 Å

60093

8zgz

EMDB-60093, PDB-8zgz:
Cryo-EM structure of inward state Anhydromuropeptide permease (AmpG)
Method: EM (single particle) / Resolution: 3.88 Å

60190

8zke

EMDB-60190, PDB-8zke:
Cryo-EM structure of inward-facing Anhydromuropeptide permease (AmpG) in complex with GlcNAc-1,6-anhMurNAc
Method: EM (single particle) / Resolution: 3.72 Å

61285

9j9z

EMDB-61285, PDB-9j9z:
Cryo-EM structure of Outward state Anhydromuropeptide permease (AmpG) complex with GlcNAc-1,6-anhMurNAc
Method: EM (single particle) / Resolution: 2.97 Å

Chemicals

ChemComp-2YP:
(2R)-2-[[(1R,2S,3R,4R,5R)-4-acetamido-2-[(2S,3R,4R,5S,6R)-3-acetamido-6-(hydroxymethyl)-4,5-bis(oxidanyl)oxan-2-yl]oxy-6,8-dioxabicyclo[3.2.1]octan-3-yl]oxy]propanoic acid

Source
  • yokenella regensburgei (Enteric Group 45)
  • homo sapiens (human)
  • synthetic construct (others)
  • escherichia coli (E. coli)
KeywordsPEPTIDE BINDING PROTEIN / transporter / ampg / cryo-em / permease / TRANSPORT PROTEIN / antibiotic resistance / membrane transporter / MEMBRANE PROTEIN / MFS / Anhydromuropeptide permease

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