7SC0
CryoEM structure of the Caveolin-1 8S complex
Summary for 7SC0
| Entry DOI | 10.2210/pdb7sc0/pdb |
| EMDB information | 25007 |
| Descriptor | Caveolin-1 (1 entity in total) |
| Functional Keywords | caveolin, caveolae, cryoem, disc, monotopic proteins, structural protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 11 |
| Total formula weight | 225440.34 |
| Authors | Porta, J.P.,Ohi, M.D.,Kenworthy, A.K.,Karakas, E. (deposition date: 2021-09-26, release date: 2022-05-25, Last modification date: 2024-06-05) |
| Primary citation | Porta, J.C.,Han, B.,Gulsevin, A.,Chung, J.M.,Peskova, Y.,Connolly, S.,Mchaourab, H.S.,Meiler, J.,Karakas, E.,Kenworthy, A.K.,Ohi, M.D. Molecular architecture of the human caveolin-1 complex. Sci Adv, 8:eabn7232-eabn7232, 2022 Cited by PubMed Abstract: Membrane-sculpting proteins shape the morphology of cell membranes and facilitate remodeling in response to physiological and environmental cues. Complexes of the monotopic membrane protein caveolin function as essential curvature-generating components of caveolae, flask-shaped invaginations that sense and respond to plasma membrane tension. However, the structural basis for caveolin's membrane remodeling activity is currently unknown. Here, we show that, using cryo-electron microscopy, the human caveolin-1 complex is composed of 11 protomers organized into a tightly packed disc with a flat membrane-embedded surface. The structural insights suggest a previously unrecognized mechanism for how membrane-sculpting proteins interact with membranes and reveal how key regions of caveolin-1, including its scaffolding, oligomerization, and intramembrane domains, contribute to its function. PubMed: 35544577DOI: 10.1126/sciadv.abn7232 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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