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TitleHow does scavenge lipids from its host membranes?
Journal, issue, pagesSci Adv, Vol. 11, Issue 40, Page eady4746, Year 2025
Publish dateOct 3, 2025
AuthorsSina Manger / Serena M Arghittu / Lasse Sprankel / Jakob Meier-Credo / Konstantin Wieland / Daniela Bublak / Julian Langer / Roberto Covino / Achilleas S Frangakis /
PubMed AbstractLipid acquisition and transport are fundamental processes in all organisms. Here, we investigate the lipid uptake and delivery mechanism of the minimal model organism . We show that the essential ...Lipid acquisition and transport are fundamental processes in all organisms. Here, we investigate the lipid uptake and delivery mechanism of the minimal model organism . We show that the essential protein P116 can transport lipids between liposomes independently and without adenosine 5'-triphosphate consumption. Our structural data and molecular dynamics simulations reveal the mechanism by which the amino-terminal region of P116 perturbs the membrane, the lipid transfer route, and the regulation of membrane binding by the cargo mass within P116's large hydrophobic cavity. When adequately filled with cargo, P116 undergoes a rapid conformational change that modulates membrane binding. Together, our results show that developed an integrated lipid uptake and delivery machinery that simplifies the complex multiprotein pathways used by higher developed organisms.
External linksSci Adv / PubMed:41032592 / PubMed Central
MethodsEM (single particle)
Resolution3.34 - 6.52 Å
Structure data

EMDB-18476: P116 (ectodomain AA 30-957) from Mycoplasma pneumoniae filled with a hydrophobic peptide.
Method: EM (single particle) / Resolution: 3.34 Å

50314

9fch

EMDB-50314: P116 (amino acids 246-818) dimer in the full state
PDB-9fch: P116 dimer in the full state (PDB structure of the full-length ectodomain truncated to amino acids 246-818)
Method: EM (single particle) / Resolution: 6.52 Å

EMDB-51408: Mycoplasma pneumoniae protein P116 ectodomain in the empty conformation
Method: EM (single particle) / Resolution: 4.36 Å

EMDB-51409: Mycoplasma pneumoniae protein P116 ectodomain in the full conformation
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-51410: Mycoplasma pneumoniae protein P116 truncated ectodomain (aa 246-818) dimer in the empty conformation
Method: EM (single particle) / Resolution: 6.52 Å

EMDB-51411: Mycoplasma pneumoniae protein P116 truncated ectodomain (aa 246-818) monomer in the empty conformation
Method: EM (single particle) / Resolution: 5.43 Å

EMDB-51412: Mycoplasma pneumoniae protein P116 truncated ectodomain (aa 246-818) monomer in the empty conformation
Method: EM (single particle) / Resolution: 5.3 Å

Source
  • mycoplasmoides pneumoniae m129 (bacteria)
KeywordsLIPID BINDING PROTEIN / Lipid Transfer Protein / Mycoplasma pneumoniae

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