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Rendering of Parkin's opening conformers resulting from molecular dynamics simulations.

Activation of Parkin by PINK1-dependent phosphorylation of Serine-65 initiates a cleft widening between the UBL domain and the adjacent linker region that propagates through release of the E2 binding region and further conformational adjustments of the active site region. The UBL domain begins its dynamic movement on the left side. Phospho-Ser65 is indicated by the 'black hole' in the UBL domain positioned on top right near the active site after its movement. See Caulfield et al.

Image Credit: Thomas R. Caulfield