7RSL

Seipin forms a flexible cage at lipid droplet formation sites

7RSL の概要

• エントリーDOI: 10.2210/pdb7rsl/pdb
• EMDBエントリー: 24674
• 分子名称: Seipin (1 entity in total)
• 機能のキーワード: lipid droplets, lipid droplet formation, complex, endoplasmic reticulum, fat storage, membrane protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 326239.53

構造登録者

Arlt, H.,Sui, X.,Folger, B.,Adams, C.,Chen, X.,Remme, R.,Hamprecht, F.A.,DiMaio, F.,Liao, M.,Goodman, J.M.,Farese Jr, R.V.,Walther, T.C. (登録日: 2021-08-11, 公開日: 2022-02-09, 最終更新日: 2024-06-05)

主引用文献

Arlt, H.,Sui, X.,Folger, B.,Adams, C.,Chen, X.,Remme, R.,Hamprecht, F.A.,DiMaio, F.,Liao, M.,Goodman, J.M.,Farese Jr., R.V.,Walther, T.C.
Seipin forms a flexible cage at lipid droplet formation sites.
Nat.Struct.Mol.Biol., 29:194-202, 2022

PubMed Abstract: Lipid droplets (LDs) form in the endoplasmic reticulum by phase separation of neutral lipids. This process is facilitated by the seipin protein complex, which consists of a ring of seipin monomers, with a yet unclear function. Here, we report a structure of S. cerevisiae seipin based on cryogenic-electron microscopy and structural modeling data. Seipin forms a decameric, cage-like structure with the lumenal domains forming a stable ring at the cage floor and transmembrane segments forming the cage sides and top. The transmembrane segments interact with adjacent monomers in two distinct, alternating conformations. These conformations result from changes in switch regions, located between the lumenal domains and the transmembrane segments, that are required for seipin function. Our data indicate a model for LD formation in which a closed seipin cage enables triacylglycerol phase separation and subsequently switches to an open conformation to allow LD growth and budding.

PubMed: 35210614
DOI: 10.1038/s41594-021-00718-y

実験手法

ELECTRON MICROSCOPY (3.45 Å)