This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6roh is a 2 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[ATC3_YEAST] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Seems to be involved in ribosome assembly. [CDC50_YEAST] Required for polarized cell growth.
Publication Abstract from PubMed
Type 4 P-type ATPases (P4-ATPases) are lipid flippases that drive the active transport of phospholipids from exoplasmic or luminal leaflets to cytosolic leaflets of eukaryotic membranes. The molecular architecture of P4-ATPases and the mechanism through which they recognize and transport lipids have remained unknown. Here we describe the cryo-electron microscopy structure of the P4-ATPase Drs2p-Cdc50p, a Saccharomyces cerevisiae lipid flippase that is specific to phosphatidylserine and phosphatidylethanolamine. Drs2p-Cdc50p is autoinhibited by the C-terminal tail of Drs2p, and activated by the lipid phosphatidylinositol-4-phosphate (PtdIns4P or PI4P). We present three structures that represent the complex in an autoinhibited, an intermediate and a fully activated state. The analysis highlights specific features of P4-ATPases and reveals sites of autoinhibition and PI4P-dependent activation. We also observe a putative lipid translocation pathway in this flippase that involves a conserved PISL motif in transmembrane segment 4 and polar residues of transmembrane segments 2 and 5, in particular Lys1018, in the centre of the lipid bilayer.
Structure and autoregulation of a P4-ATPase lipid flippase.,Timcenko M, Lyons JA, Januliene D, Ulstrup JJ, Dieudonne T, Montigny C, Ash MR, Karlsen JL, Boesen T, Kuhlbrandt W, Lenoir G, Moeller A, Nissen P Nature. 2019 Jun 26. pii: 10.1038/s41586-019-1344-7. doi:, 10.1038/s41586-019-1344-7. PMID:31243363[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Timcenko M, Lyons JA, Januliene D, Ulstrup JJ, Dieudonne T, Montigny C, Ash MR, Karlsen JL, Boesen T, Kuhlbrandt W, Lenoir G, Moeller A, Nissen P. Structure and autoregulation of a P4-ATPase lipid flippase. Nature. 2019 Jun 26. pii: 10.1038/s41586-019-1344-7. doi:, 10.1038/s41586-019-1344-7. PMID:31243363 doi:http://dx.doi.org/10.1038/s41586-019-1344-7
