8a9b

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

spinqualitylabelsall models 8a9b, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8a9b is a 1 chain structure with sequence from Mycoplasma pneumoniae M129. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Y213_MYCPN Publication Abstract from PubMed 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. Essential protein P116 extracts cholesterol and other indispensable lipids for Mycoplasmas.,Sprankel L, Vizarraga D, Martin J, Manger S, Meier-Credo J, Marcos M, Julve J, Rotllan N, Scheffer MP, Escola-Gil JC, Langer JD, Pinol J, Fita I, Frangakis AS Nat Struct Mol Biol. 2023 Mar;30(3):321-329. doi: 10.1038/s41594-023-00922-y. , Epub 2023 Feb 13. PMID:36782049 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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