6DS5
Cryo EM structure of human SEIPIN
Summary for 6DS5
| Entry DOI | 10.2210/pdb6ds5/pdb |
| EMDB information | 8909 |
| Descriptor | Seipin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | lipid droplets, adipogenesis, lipid binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 11 |
| Total formula weight | 508177.56 |
| Authors | Yan, R.H.,Qian, H.W.,Yan, N.,Yang, H.Y. (deposition date: 2018-06-13, release date: 2018-10-24, Last modification date: 2024-11-13) |
| Primary citation | Yan, R.,Qian, H.,Lukmantara, I.,Gao, M.,Du, X.,Yan, N.,Yang, H. Human SEIPIN Binds Anionic Phospholipids. Dev. Cell, 47:248-256.e4, 2018 Cited by PubMed Abstract: The biogenesis of lipid droplets (LDs) and the development of adipocytes are two key aspects of mammalian fat storage. SEIPIN, an integral membrane protein of the endoplasmic reticulum (ER), plays a critical role in both LD formation and adipogenesis. The molecular function of SEIPIN, however, has yet to be elucidated. Here, we report the cryogenic electron microscopy structure of human SEIPIN at 3.8 Å resolution. SEIPIN exists as an undecamer, and this oligomerization state is critical for its physiological function. The evolutionarily conserved lumenal domain of SEIPIN forms an eight-stranded β sandwich fold. Both full-length SEIPIN and its lumenal domain can bind anionic phospholipids including phosphatidic acid. Our results suggest that SEIPIN forms a scaffold that helps maintain phospholipid homeostasis and surface tension of the ER. PubMed: 30293840DOI: 10.1016/j.devcel.2018.09.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
Download full validation report
