6MLU
Cryo-EM structure of lipid droplet formation protein Seipin/BSCL2
Summary for 6MLU
| Entry DOI | 10.2210/pdb6mlu/pdb |
| EMDB information | 9146 |
| Descriptor | Seipin (1 entity in total) |
| Functional Keywords | lipid storage, lipid droplet formation, lipodystrophy, membrane protein |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 2 |
| Total formula weight | 87914.14 |
| Authors | Sui, X.,Arlt, H.,Liao, M.,Walther, C.T.,Farese, V.R. (deposition date: 2018-09-28, release date: 2018-10-17, Last modification date: 2024-11-13) |
| Primary citation | Sui, X.,Arlt, H.,Brock, K.P.,Lai, Z.W.,DiMaio, F.,Marks, D.S.,Liao, M.,Farese Jr., R.V.,Walther, T.C. Cryo-electron microscopy structure of the lipid droplet-formation protein seipin. J. Cell Biol., 217:4080-4091, 2018 Cited by PubMed Abstract: Metabolic energy is stored in cells primarily as triacylglycerols in lipid droplets (LDs), and LD dysregulation leads to metabolic diseases. The formation of monolayer-bound LDs from the endoplasmic reticulum (ER) bilayer is poorly understood, but the ER protein seipin is essential to this process. In this study, we report a cryo-electron microscopy structure and functional characterization of seipin. The structure reveals a ring-shaped dodecamer with the luminal domain of each monomer resolved at ∼4.0 Å. Each luminal domain monomer exhibits two distinctive features: a hydrophobic helix (HH) positioned toward the ER bilayer and a β-sandwich domain with structural similarity to lipid-binding proteins. This structure and our functional testing in cells suggest a model in which seipin oligomers initially detect forming LDs in the ER via HHs and subsequently act as membrane anchors to enable lipid transfer and LD growth. PubMed: 30327422DOI: 10.1083/jcb.201809067 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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