7DRX
Cryo-EM structure of Dnf1 from Saccharomyces cerevisiae in 90PS with beryllium fluoride (E2P state)
Summary for 7DRX
| Entry DOI | 10.2210/pdb7drx/pdb |
| EMDB information | 30829 |
| Descriptor | 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, ... (6 entities in total) |
| Functional Keywords | p4-atpases, lipid transport |
| Biological source | Saccharomyces cerevisiae S288C More |
| Total number of polymer chains | 2 |
| Total formula weight | 227693.62 |
| Authors | |
| Primary citation | Xu, J.,He, Y.,Wu, X.,Li, L. Conformational changes of a phosphatidylcholine flippase in lipid membranes. Cell Rep, 38:110518-110518, 2022 Cited by 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: 35294892DOI: 10.1016/j.celrep.2022.110518 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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