6DS5

Cryo EM structure of human SEIPIN

6DS5 の概要

• エントリーDOI: 10.2210/pdb6ds5/pdb
• EMDBエントリー: 8909
• 分子名称: Seipin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: lipid droplets, adipogenesis, lipid binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 508177.56

構造登録者

Yan, R.H.,Qian, H.W.,Yan, N.,Yang, H.Y. (登録日: 2018-06-13, 公開日: 2018-10-24, 最終更新日: 2025-05-28)

主引用文献

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

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: 30293840
DOI: 10.1016/j.devcel.2018.09.010

実験手法

ELECTRON MICROSCOPY (3.8 Å)