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TitleStructural basis of lipopolysaccharide assembly by the outer membrane translocon holo-complex.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 10404, Year 2025
Publish dateNov 24, 2025
AuthorsHaoxiang Chen / Axel Siroy / Violette Morales / Dominik Gurvič / Yves Quentin / Stephanie Balor / Yassin A Abuta'a / Maurine Marteau / Carine Froment / Anne Caumont-Sarcos / Julien Marcoux / Phillip J Stansfeld / Rémi Fronzes / Raffaele Ieva /
PubMed AbstractLipopolysaccharide (LPS) assembly at the surfaces-exposed leaflet of the bacterial outer membrane (OM) is mediated by the OM LPS translocon. An essential transmembrane β-barrel protein, LptD, and a ...Lipopolysaccharide (LPS) assembly at the surfaces-exposed leaflet of the bacterial outer membrane (OM) is mediated by the OM LPS translocon. An essential transmembrane β-barrel protein, LptD, and a cognate lipoprotein, LptE, translocate LPS selectively into the OM external leaflet via a poorly understood mechanism. Here, we characterize two additional translocon subunits, the lipoproteins LptM and LptY (formerly YedD). We use single-particle cryo-EM analysis, functional assays and molecular dynamics simulations to visualize the roles of LptM and LptY at the translocon holo-complex LptDEMY, uncovering their impact on LptD conformational dynamics. Whereas LptY binds and stabilizes the periplasmic LptD β-taco domain that functions as LPS receptor, LptM intercalates the lateral gate of the β-barrel domain, promoting its opening and access by LPS. Remarkably, we demonstrate a conformational switch of the LptD β-taco/β-barrel interface alternating between contracted and extended states. β-strand 1 of LptD, which defines the mobile side of the lateral gate, binds LPS and performs a stroke movement toward the external leaflet during the contracted-to-extended state transition. Our findings support a detailed mechanistic framework explaining the selective transport of LPS to the membrane external leaflet.
External linksNat Commun / PubMed:41285762 / PubMed Central
MethodsEM (single particle)
Resolution2.47 - 2.74 Å
Structure data

52773

9i9z

EMDB-52773, PDB-9i9z:
LpDE from Escherichia coli
Method: EM (single particle) / Resolution: 2.74 Å

52777

9ia0

EMDB-52777, PDB-9ia0:
LpDE from Escherichia coli
Method: EM (single particle) / Resolution: 2.62 Å

52778

9ia2

EMDB-52778, PDB-9ia2:
LpDEM from Escherichia coli
Method: EM (single particle) / Resolution: 2.47 Å

52779

9ia5

EMDB-52779, PDB-9ia5:
LpDEM from Escherichia coli
Method: EM (single particle) / Resolution: 2.63 Å

Source
  • escherichia coli (E. coli)
KeywordsTRANSPORT PROTEIN / Lipopolysaccharide transport

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