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TitleEssential protein P116 extracts cholesterol and other indispensable lipids for Mycoplasmas.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 3, Page 321-329, Year 2023
Publish dateFeb 13, 2023
AuthorsLasse Sprankel / David Vizarraga / Jesús Martín / Sina Manger / Jakob Meier-Credo / Marina Marcos / Josep Julve / Noemi Rotllan / Margot P Scheffer / Joan Carles Escolà-Gil / Julian D Langer / Jaume Piñol / Ignacio Fita / Achilleas S Frangakis /
PubMed AbstractMycoplasma pneumoniae, responsible for approximately 30% of community-acquired human pneumonia, needs to extract lipids from the host environment for survival and proliferation. Here, we report a ...Mycoplasma pneumoniae, responsible for approximately 30% of community-acquired human pneumonia, needs to extract lipids from the host environment for survival and proliferation. Here, we report a comprehensive structural and functional analysis of the previously uncharacterized protein P116 (MPN_213). Single-particle cryo-electron microscopy of P116 reveals a homodimer presenting a previously unseen fold, forming a huge hydrophobic cavity, which is fully accessible to solvent. Lipidomics analysis shows that P116 specifically extracts lipids such as phosphatidylcholine, sphingomyelin and cholesterol. Structures of different conformational states reveal the mechanism by which lipids are extracted. This finding immediately suggests a way to control Mycoplasma infection by interfering with lipid uptake.
External linksNat Struct Mol Biol / PubMed:36782049 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 9.0 Å
Structure data

15274

8a9a

EMDB-15274, PDB-8a9a:
Single Particle cryo-EM of the lipid binding protein P116 (MPN213) from Mycoplasma pneumoniae at 3.3 Angstrom resolution.
Method: EM (single particle) / Resolution: 3.3 Å

15275

8a9b

EMDB-15275, PDB-8a9b:
Single Particle cryo-EM of the empty lipid binding protein P116 (MPN213) from Mycoplasma pneumoniae at 4 Angstrom resolution
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-15276: Single Particle cryo-EM of the lipid binding protein P116 (MPN213) refilled with FBS from Mycoplasma pneumoniae at 3.5 Angstrom resolution.
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-15277: Single Particle cryo-EM of the lipid binding protein P116 (MPN213) from Mycoplasma pneumoniae bound to HDL.
Method: EM (single particle) / Resolution: 9.0 Å

Source
  • mycoplasma pneumoniae m129 (bacteria)
KeywordsLIPID BINDING PROTEIN / Lipid binding protein P116 (MPN213) from Mycoplasma pneumoniae / LIPID BINDING / Empty lipid binding protein P116 (MPN213) from Mycoplasma pneumoniae

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