8A9B

Single Particle cryo-EM of the empty lipid binding protein P116 (MPN213) from Mycoplasma pneumoniae at 4 Angstrom resolution

Summary for 8A9B

• Entry DOI: 10.2210/pdb8a9b/pdb
• Related: 8A9A
• EMDB information: 15274 15275
• Descriptor: Lipid binding protein P116 (MPN213) (1 entity in total)
• Functional Keywords: empty lipid binding protein p116 (mpn213) from mycoplasma pneumoniae, lipid binding, lipid binding protein
• Biological source: Mycoplasma pneumoniae M129
• Total number of polymer chains: 1
• Total formula weight: 114149.85

Authors

Sprankel, L.,Vizarraga, D. (deposition date: 2022-06-28, release date: 2023-02-22, Last modification date: 2024-07-24)

Primary citation

Sprankel, L.,Vizarraga, D.,Martin, J.,Manger, S.,Meier-Credo, J.,Marcos, M.,Julve, J.,Rotllan, N.,Scheffer, M.P.,Escola-Gil, J.C.,Langer, J.D.,Pinol, J.,Fita, I.,Frangakis, A.S.
Essential protein P116 extracts cholesterol and other indispensable lipids for Mycoplasmas.
Nat.Struct.Mol.Biol., 30:321-329, 2023

PubMed Abstract: 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.

PubMed: 36782049
DOI: 10.1038/s41594-023-00922-y

Experimental method

ELECTRON MICROSCOPY (4 Å)