9FCH

P116 dimer in the full state (PDB structure of the full-length ectodomain truncated to amino acids 246-818)

これはPDB形式変換不可エントリーです。

9FCH の概要

• エントリーDOI: 10.2210/pdb9fch/pdb
• 関連するPDBエントリー: 8a9a 8a9b
• EMDBエントリー: 18478 50314
• 分子名称: Uncharacterized protein MG075 homolog (1 entity in total)
• 機能のキーワード: lipid transfer protein, mycoplasma pneumoniae, lipid binding protein
• 由来する生物種: Mycoplasmoides pneumoniae M129
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 128773.50

構造登録者

Mager, S. (登録日: 2024-05-15, 公開日: 2024-05-29, 最終更新日: 2025-10-22)

主引用文献

Manger, S.,Arghittu, S.M.,Sprankel, L.,Meier-Credo, J.,Wieland, K.,Bublak, D.,Langer, J.,Covino, R.,Frangakis, A.S.
How does Mycoplasma pneumoniae scavenge lipids from its host membranes?
Sci Adv, 11:eady4746-eady4746, 2025

PubMed Abstract: 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.

PubMed: 41032592
DOI: 10.1126/sciadv.ady4746

実験手法

ELECTRON MICROSCOPY (6.52 Å)