Fig. 8.

Modeling of the active conformation of Atg3~Atg8 intermediate. a Generation of model for a potential closed E2~Ubl conformation for Atg3~Atg8, with structures of Atg3^∆NFR (PDB 6OJJ, from this study) and Atg8 (PDB 2ZPN) superimposed on E2 and Ub, respectively, in a RING E3–E2–Ub complex (PDB 4AP4). b Sites of Atg3 mutations impairing E3-dependent activation of Atg3~Atg8, mapped on model for closed conformation. Red—residues corresponding to E2–Ub interface in closed conformation; wheat—residues corresponding to RING E3-binding site; bronze—residues in catalytic segment. c Sites of Atg8 mutations impairing E3-dependent activation of Atg3~Atg8, mapped on model for closed conformation. Red—residues corresponding to E2–Ub interface in closed conformation; orange—residues corresponding to AIM/LIR-binding site. d Atg8 residues showing chemical shift perturbation one standard deviation above the mean upon covalent complex formation with Atg3, mapped on model for closed conformation. Red—residues corresponding to E2–Ub interface in closed conformation; orange—residues corresponding to AIM/LIR-binding site