Figure 1 | Scientific Reports

Figure 1

From: Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding

Figure 1

Pichia angusta Atg18 structure. (A) Cartoon representations of Atg18 rainbow-colored from blue at the N-terminus to red at the C-terminus. The ligands and FRRG arginine side chains are shown as ball and sticks. Loop 6CD (297–437) is missing and marked through the last ordered residues 296 and 438. Panels (AC) show the protein in the same orientation. Surface representations of Atg18 showing (B) surface charges with blue depicting positive and red negative charges and (C) conservation of the molecule. Conservation analysis was done with Consurf46. Proteins used for the sequence alignment are listed in the Methods section. (D) Close up on site 1 with bound citrate. The omit mFo-DFc difference map, where m is the figure of merit and D the sigma A weighting factor has a contour level of σ = +2.5. Scheme showing ligand protein interactions was adapted from LigPlot+. Hydrogen bonds and salt bridges between ligand and protein are shown with dashed lines and distances are given in Ångstrom. Water molecules are depicted as cyan spheres. (E) Site 1 with a bound phosphate ion. The 2.5 Å resolution 2mFo-DFc map is contoured at 1.0 σ. (F) PIP binding site 2 with a bound phosphate ion. The 2.0 Å resolution 2mFo-DFc electron density map is contoured at 1.0 σ. Residues with disordered side chains are marked with an asterisk.