8A9B

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

8A9B の概要

• エントリーDOI: 10.2210/pdb8a9b/pdb
• 関連するPDBエントリー: 8A9A
• EMDBエントリー: 15274 15275
• 分子名称: Lipid binding protein P116 (MPN213) (1 entity in total)
• 機能のキーワード: empty lipid binding protein p116 (mpn213) from mycoplasma pneumoniae, lipid binding, lipid binding protein
• 由来する生物種: Mycoplasma pneumoniae M129
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 114149.85

構造登録者

Sprankel, L.,Vizarraga, D. (登録日: 2022-06-28, 公開日: 2023-02-22, 最終更新日: 2025-07-09)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (4 Å)