Fig. 3: GPI binds GPI-T with a rich network of interactions.
From: Structures of liganded glycosylphosphatidylinositol transamidase illuminate GPI-AP biogenesis
a Interactions between GPI (stick) and GPI-TC206S (cylinder-cartoon with interacting residues in stick representations) (GPAA1, pink; PIGT, orange; PIGU, cyan). The cryo-EM density of GPI is represented by a transparent grey surface. H-bonds/metal coordination with distances in Å are indicated by dash lines. GPI is colored alternatingly for better visualization. The catalytic dyad residue His164 (blue sphere) and proULBP2 (green cartoon) are shown for orientation purposes. An asterisk on Man3 indicates the 2-hydroxyl where a fourth mannose may be added. b Simplified LigPlot72 view of the GPI-enzyme interactions. Hydrophobic interactions are indicated by eye slashes and H-bonds/metal coordinations are indicated by dashed lines. GPI is colored alternatively and protein subunits are shaded differently as indicated. GPI-T subunits and proULBP2 are color-coded as in a. EtNP, ethanolamine phosphate; GlcN, glucosamine; Ino, inositol; Man, mannose. c Apparent activity of GPAA1 Q355P. Surface staining of the two GPI-AP markers (CD59, left; PrP, right) in GPAA1 knockout cells expressing Q355P (red) or the wild-type GPAA1 (black) using fluorescence-activated cell sorting. Typical results from three independent experiments are shown. See Supplementary Fig. 15b for the gating strategy. Source data are provided as a Source Data file.
