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. 2018 Nov 14;4(11):eaau6044. doi: 10.1126/sciadv.aau6044

Fig. 2. GM:PP1 holoenzyme structure.

Fig. 2

(A) Crystal structure of GM64–93:PP1α7–300. GM64–93 shown in pink with a 2Fo − Fc electron density map contoured at 1σ (2 Å) and PP1 shown as surface (gray). RVxF binding pocket (cyan), ΦΦ binding pocket (salmon), and the active site (orange) of PP1 are highlighted. PP1 substrate binding grooves (A, acidic; H, hydrophobic; C, C-terminal) are marked. (B) Close-up of GM bound to PP1. GM residues 65RVSF68 bind the PP1 RVxF binding pocket (cyan), and GM residues 79VK80 bind the PP1 ΦΦ binding pocket (salmon). (C) GM residues 78 to 81 form a β strand (green) to cap β strand 14 of PP1 via hydrogen bonds (dotted blue lines). (D) Greek key turn residues (raspberry), D70GM:R261PP1 salt bridge (yellow dotted lines), L76GM (lid), and F82GM are shown as sticks; ΦR pocket is highlighted.