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. Author manuscript; available in PMC: 2016 Jun 30.
Published in final edited form as: Cell Rep. 2015 Jun 18;11(12):1885–1891. doi: 10.1016/j.celrep.2015.05.043

Figure 2. The 3D structure of the GADD34:PP1 holoenzyme.

Figure 2

(a) GADD34 (residues 553-568, light blue, electron density 2Fo-Fc contoured at 1σ) and PP1α7-300 (gray, surface) form a complex. Two Mn2+ ions (pink spheres) are bound at the PP1 active site; bound phosphate is shown as sticks. No electron density was observed for GADD34 residues 552 or 569-591. (b) GADD34 PP1-binding domain with the two primary interaction sites (RVxF and ΦΦ residues are shown as sticks) highlighted. (c) SDS-PAGE of ~20 GADD34552-591:PP1α7-300 crystals; comparable migration of GADD34 from crystals and control (GADD34552-591 alone) shows that no proteolytic degradation of GADD34552-591 occurred during crystallization. (d) ITC of GADD34552-567 and PP1α7-330.