Extended Data Fig. 5: Detailed analysis of the β5-propeptide.
From: Mechanism of autocatalytic activation during proteasome assembly
a, Comparison of β5 between mature wild-type 20S (PDB: 5CZ4) and the β3-D205Δ preholoproteasome. The mature portions of β5 largely overlap, although there is a slight rotation of β5 towards the CP midline in the mature 20S, which may reflect final tightening of the CP upon completion of assembly. The first and last resolved residues are indicated. b, Overlay of the two structures from panel A, highlighting the differences between them. Arrows designate portions of β5 that are unresolved in preholoproteasome. c, Overlay of the molecular model of the β5-propeptide onto its primary map density, confirming the validity of the model. Boxed panels show close-up views of selected regions and arrows indicate their position in the overall propeptide.
