8GYW

Cryo-EM structure of human CEPT1 complexed with CDP-choline

8GYW の概要

• エントリーDOI: 10.2210/pdb8gyw/pdb
• EMDBエントリー: 34378
• 分子名称: Choline/ethanolaminephosphotransferase 1, MAGNESIUM ION, [2-CYTIDYLATE-O'-PHOSPHONYLOXYL]-ETHYL-TRIMETHYL-AMMONIUM (3 entities in total)
• 機能のキーワード: cept1, choline/ethanolamine phosphotransferase, lipid binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86464.05

構造登録者

Qian, H.W.,Wang, Z.H. (登録日: 2022-09-24, 公開日: 2023-03-22, 最終更新日: 2025-07-02)

主引用文献

Wang, Z.,Yang, M.,Yang, Y.,He, Y.,Qian, H.
Structural basis for catalysis of human choline/ethanolamine phosphotransferase 1.
Nat Commun, 14:2529-2529, 2023

PubMed Abstract: Phosphatidylcholine (PC) and phosphatidylethanolamine (PE) are two primary components of the eukaryotic membrane and play essential roles in the maintenance of membrane integrity, lipid droplet biogenesis, autophagosome formation, and lipoprotein formation and secretion. Choline/ethanolamine phosphotransferase 1 (CEPT1) catalyzes the last step of the biosynthesis of PC and PE in the Kennedy pathway by transferring the substituted phosphate group from CDP-choline/ethanolamine to diacylglycerol. Here, we present the cryo-EM structures of human CEPT1 and its complex with CDP-choline at resolutions of 3.7 Å and 3.8 Å, respectively. CEPT1 is a dimer with 10 transmembrane segments (TMs) in each protomer. TMs 1-6 constitute a conserved catalytic domain with an interior hydrophobic chamber accommodating a PC-like density. Structural observations and biochemical characterizations suggest that the hydrophobic chamber coordinates the acyl tails during the catalytic process. The PC-like density disappears in the structure of the complex with CDP-choline, suggesting a potential substrate-triggered product release mechanism.

PubMed: 37137909
DOI: 10.1038/s41467-023-38290-2

実験手法

ELECTRON MICROSCOPY (3.9 Å)