7dsh
From Proteopedia
Cryo-EM structure of Dnf1 from Saccharomyces cerevisiae in 90PS with AMPPCP (E1-ATP state)
Structural highlights
FunctionATC5_YEAST Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide, phosphatidylcholine, phosphatidylethanolamine, and small amounts of phosphatidylserine from the lumenal to the cytosolic leaflet of the cell membrane and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:12631737, PubMed:22308393, PubMed:22791719, PubMed:23302692, PubMed:31786280, PubMed:33060204, PubMed:33320091, PubMed:35294892). Does not appear to transport sphingomyelin, inositol phosphoceramide, or phosphatidic acid (PubMed:12631737, PubMed:22308393, PubMed:33320091). Required for efficient endocytosis (PubMed:12631737).[1] [2] [3] [4] [5] [6] [7] [8] Publication Abstract from PubMedType 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. Conformational changes of a phosphatidylcholine flippase in lipid membranes.,Xu J, He Y, Wu X, Li L Cell Rep. 2022 Mar 15;38(11):110518. doi: 10.1016/j.celrep.2022.110518. PMID:35294892[9] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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