9hdh

Structure of s.c.Osh6 in complex with Ist2 732-761 and POPS

spinqualitylabelsall models 9hdh, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9hdh is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.84Å Ligands: P5S Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function OSH6_YEAST Publication Abstract from PubMed Membrane contact sites are hubs for interorganellar lipid transport within eukaryotic cells. As a principal tether bridging the endoplasmic reticulum (ER) and the plasma membrane in Saccharomyces cerevisiae, the protein IST2 has a major role during lipid transport between both compartments. Here, we show a comprehensive investigation elucidating the structural and mechanistic properties of IST2 and its interaction with the soluble lipid transfer protein OSH6. The ER-embedded transmembrane domain of IST2 is homologous to the TMEM16 family and acts as a constitutively active lipid scramblase. The extended C terminus binds to the plasma membrane and the phosphatidylserine-phosphatidylinositol 4-phosphate exchanger OSH6. Through cellular growth assays and biochemical and structural studies, we characterized the interaction between both proteins and show that OSH6 remains associated with IST2 during lipid shuttling between membranes. These results highlight the role of the IST2-OSH6 complex in lipid trafficking and offer initial insights into the relevance of scramblases for carrier-like lipid transport mechanisms. Structural basis for lipid transport at membrane contact sites by the IST2-OSH6 complex.,Arndt M, Schweri A, Dutzler R Nat Struct Mol Biol. 2025 Aug 27. doi: 10.1038/s41594-025-01660-z. PMID:40866577 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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