6MLU

Cryo-EM structure of lipid droplet formation protein Seipin/BSCL2

6MLU の概要

• エントリーDOI: 10.2210/pdb6mlu/pdb
• EMDBエントリー: 9146
• 分子名称: Seipin (1 entity in total)
• 機能のキーワード: lipid storage, lipid droplet formation, lipodystrophy, membrane protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87914.14

構造登録者

Sui, X.,Arlt, H.,Liao, M.,Walther, C.T.,Farese, V.R. (登録日: 2018-09-28, 公開日: 2018-10-17, 最終更新日: 2024-11-13)

主引用文献

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

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: 30327422
DOI: 10.1083/jcb.201809067

実験手法

ELECTRON MICROSCOPY (4 Å)