Extended Data Figure 6: Structural detail and B-factor analysis.

a, PhosphoUb-induced pUBH straightening is energetically neutral as the two hydrogen bonds between helix residues and the RING1 core are not lost but only adjusted. Left: full-length RnPARKIN structure (PDB 4K95 (ref. 16)). Right: PhPARKIN–pUb structure. b, Structure of full-length RnPARKIN (PDB 4K95 (ref. 16), left), PhPARKIN–pUb (middle), and a superposition of the two (right), in which Cα atoms of structurally identical, ordered residues of the IBR–REP linker are shown as spheres. The distance between these residues is indicated by a dotted line. The linker sequence is highlighted in Extended Data Fig. 2. c, Structures of PARKIN in which B-factors were refined for individual atoms (PDB 4BM9 (ref. 14); 4I1H (ref. 15)) are shown in a ribbon representation, in which the ribbon thickness indicates B-factors differences, with thin ribbons indicating low and thick ribbon indicating high B-factors. The full-length RnPARKIN structure (PDB 4K95 (ref. 16)) is not included as in this 6.5 Å structure overall B-factors were assigned. d, Structures of PhPARKIN–pUb are shown as in c for each molecule of the asymmetric unit. The REP and RING2 elements are destabilized as indicated by higher B-factors. The rigid core of the protein has shifted from the UPD–RING1–RING2 interfaces (compare c) to the UPD–RING1–IBR–phosphoUb interfaces. B-factor analysis may be distorted by neighbouring molecules and crystal contacts, which are not indicated here.