Fig. 1: Structure of human XPR1 in the closed state.
From: Synergistic activation of the human phosphate exporter XPR1 by KIDINS220 and inositol pyrophosphate
Cryo-EM maps (a) and structural models (b) of the closed state XPR1 (XPR1C) from the side view, extracellular view, and intracellular view. The two protomers are colored light pink and light green. Lipids are shown in magenta. The approximate boundaries of the phospholipid bilayer are indicated as thick black lines. The outward cavity and intracellular cavity are labeled from the extracellular view and intracellular view in (b). c Schematic diagram of the secondary structure features of XPR1’s TMD. The Glu622/Phe623 motif near the C-terminal of XPR1 is labeled in purple. d The potential disulfide bond between C415 and C440. e Cryo-EM density map of the cholesterol at the pocket formed by TM2, TM9, and TM10, which is shown as blue meshes. f Cryo-EM density map of the lipid at the pocket formed by TM2, TM4, H2, and TM5, which is shown as blue meshes.
