7p16

Structure of caspase-3 cleaved rXKR9 in complex with a sybody at 4.3A

spinqualitylabelsall models 7p16, resolution 4.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7p16 is a 2 chain structure with sequence from Rattus norvegicus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.3Å Ligands: PLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5GH54_RAT Publication Abstract from PubMed The exposure of the negatively charged lipid phosphatidylserine on the cell surface, catalyzed by lipid scramblases, is an important signal for the clearance of apoptotic cells by macrophages. The protein XKR9 is a member of a conserved family that has been associated with apoptotic lipid scrambling. Here, we describe structures of full-length and caspase-treated XKR9 from Rattus norvegicus in complex with a synthetic nanobody determined by cryo-electron microscopy. The 43 kDa monomeric membrane protein can be divided into two structurally related repeats, each containing four membrane-spanning segments and a helix that is partly inserted into the lipid bilayer. In the full-length protein, the C-terminus interacts with a hydrophobic pocket located at the intracellular side acting as an inhibitor of protein function. Cleavage by caspase-3 at a specific site releases 16 residues of the C-terminus, thus making the pocket accessible to the cytoplasm. Collectively, the work has revealed the unknown architecture of the XKR family and has provided initial insight into its activation by caspases. Cryo-EM structures of the caspase-activated protein XKR9 involved in apoptotic lipid scrambling.,Straub MS, Alvadia C, Sawicka M, Dutzler R Elife. 2021 Jul 15;10:e69800. doi: 10.7554/eLife.69800. PMID:34263724 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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