7DSH

Cryo-EM structure of Dnf1 from Saccharomyces cerevisiae in 90PS with AMPPCP (E1-ATP state)

7DSH の概要

• エントリーDOI: 10.2210/pdb7dsh/pdb
• EMDBエントリー: 30833
• 分子名称: Phospholipid-transporting ATPase DNF1, Alkylphosphocholine resistance protein LEM3, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: p4-atpases, lipid transport
• 由来する生物種: Saccharomyces cerevisiae S288C; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 226606.62

構造登録者

Xu, J.,He, Y.,Wu, X.,Li, L. (登録日: 2020-12-31, 公開日: 2022-03-23, 最終更新日: 2025-06-25)

主引用文献

Xu, J.,He, Y.,Wu, X.,Li, L.
Conformational changes of a phosphatidylcholine flippase in lipid membranes.
Cell Rep, 38:110518-110518, 2022

PubMed Abstract: Type 4 P-type ATPases (P4-ATPases) actively and selectively translocate phospholipids across membrane bilayers. Driven by ATP hydrolysis, P4-ATPases undergo conformational changes during lipid flipping. It is unclear how the active flipping states of P4-ATPases are regulated in the lipid membranes, especially for phosphatidylcholine (PC)-flipping P4-ATPases whose substrate, PC, is a substantial component of membranes. Here, we report the cryoelectron microscopy structures of a yeast PC-flipping P4-ATPase, Dnf1, in lipid environments. In native yeast lipids, Dnf1 adopts a conformation in which the lipid flipping pathway is disrupted. Only when the lipid composition is changed can Dnf1 be captured in the active conformations that enable lipid flipping. These results suggest that, in the native membrane, Dnf1 may stay in an idle conformation that is unable to support the trans-membrane movement of lipids. Dnf1 may have altered conformational preferences in membranes with different lipid compositions.

PubMed: 35294892
DOI: 10.1016/j.celrep.2022.110518

実験手法

ELECTRON MICROSCOPY (3.67 Å)