EMD-31487

Single-particle
3.81 Å
EMD-31487 Deposition: 29/06/2021
Map released: 23/03/2022
Last modified: 09/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-31487

Cryo-EM structure of Dnf1 from Saccharomyces cerevisiae in yeast lipids with beryllium fluoride (resting state)

EMD-31487

Single-particle
3.81 Å
EMD-31487 Deposition: 29/06/2021
Map released: 23/03/2022
Last modified: 09/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharomyces cerevisiae S288C
Sample: Dnf1_Lem3 complex
Fitted models: 7f7f (Avg. Q-score: 0.379)

Deposition Authors: Xu J, He Y
Conformational changes of a phosphatidylcholine flippase in lipid membranes.
Xu J, He Y , Wu X, Li L
(2022) Cell Rep , 38 , 110518 - 110518
PUBMED: 35294892
DOI: doi:10.1016/j.celrep.2022.110518
ISSN: 2211-1247
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.