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TitleAutoinhibition and activation mechanisms of the eukaryotic lipid flippase Drs2p-Cdc50p.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 4142, Year 2019
Publish dateSep 12, 2019
AuthorsLin Bai / Amanda Kovach / Qinglong You / Hao-Chi Hsu / Gongpu Zhao / Huilin Li /
PubMed AbstractThe heterodimeric eukaryotic Drs2p-Cdc50p complex is a lipid flippase that maintains cell membrane asymmetry. The enzyme complex exists in an autoinhibited form in the absence of an activator and is ...The heterodimeric eukaryotic Drs2p-Cdc50p complex is a lipid flippase that maintains cell membrane asymmetry. The enzyme complex exists in an autoinhibited form in the absence of an activator and is specifically activated by phosphatidylinositol-4-phosphate (PI4P), although the underlying mechanisms have been unclear. Here we report the cryo-EM structures of intact Drs2p-Cdc50p isolated from S. cerevisiae in apo form and in the PI4P-activated form at 2.8 Å and 3.3 Å resolution, respectively. The structures reveal that the Drs2p C-terminus lines a long groove in the cytosolic regulatory region to inhibit the flippase activity. PIP4 binding in a cytosol-proximal membrane region triggers a 90° rotation of a cytosolic helix switch that is located just upstream of the inhibitory C-terminal peptide. The rotation of the helix switch dislodges the C-terminus from the regulatory region, activating the flippase.
External linksNat Commun / PubMed:31515475 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.3 Å
Structure data

20467

6psx

EMDB-20467, PDB-6psx:
Cryo-EM structure of S. cerevisiae Drs2p-Cdc50p in the PI4P-activated form
Method: EM (single particle) / Resolution: 3.3 Å

20468

6psy

EMDB-20468, PDB-6psy:
Cryo-EM structure of S. cerevisiae Drs2p-Cdc50p in the autoinhibited apo form
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • saccharomyces cerevisiae w303 (yeast)
KeywordsTRANSLOCASE / complex / phospholipid flippase / P-type ATPase

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