9FCH

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

This is a non-PDB format compatible entry.

Summary for 9FCH

• Entry DOI: 10.2210/pdb9fch/pdb
• Related: 8a9a 8a9b
• EMDB information: 18478 50314
• Descriptor: Uncharacterized protein MG075 homolog (1 entity in total)
• Functional Keywords: lipid transfer protein, mycoplasma pneumoniae, lipid binding protein
• Biological source: Mycoplasmoides pneumoniae M129
• Total number of polymer chains: 2
• Total formula weight: 128773.50

Authors

Mager, S. (deposition date: 2024-05-15, release date: 2024-05-29, Last modification date: 2025-10-22)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (6.52 Å)