9BQ2
Structure of the flotillin complex in a native membrane environment
Summary for 9BQ2
| Entry DOI | 10.2210/pdb9bq2/pdb |
| EMDB information | 44792 |
| Descriptor | Flotillin-2, Flotillin-1 (2 entities in total) |
| Functional Keywords | flotillin complex, spfh, membrane interaction, endocytosis, membrane protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 91452.77 |
| Authors | |
| Primary citation | Fu, Z.,MacKinnon, R. Structure of the flotillin complex in a native membrane environment. Proc.Natl.Acad.Sci.USA, 121:e2409334121-e2409334121, 2024 Cited by PubMed Abstract: In this study, we used cryoelectron microscopy to determine the structures of the Flotillin protein complex, part of the Stomatin, Prohibitin, Flotillin, and HflK/C (SPFH) superfamily, from cell-derived vesicles without detergents. It forms a right-handed helical barrel consisting of 22 pairs of Flotillin1 and Flotillin2 subunits, with a diameter of 32 nm at its wider end and 19 nm at its narrower end. Oligomerization is stabilized by the C terminus, which forms two helical layers linked by a β-strand, and coiled-coil domains that enable strong charge-charge intersubunit interactions. Flotillin interacts with membranes at both ends; through its SPFH1 domains at the wide end and the C terminus at the narrow end, facilitated by hydrophobic interactions and lipidation. The inward tilting of the SPFH domain, likely triggered by phosphorylation, suggests its role in membrane curvature induction, which could be connected to its proposed role in clathrin-independent endocytosis. The structure suggests a shared architecture across the family of SPFH proteins and will promote further research into Flotillin's roles in cell biology. PubMed: 38985763DOI: 10.1073/pnas.2409334121 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
Download full validation report
