Figure 5
From: Cryo-EM structure of SKP1-SKP2-CKS1 in complex with CDK2-cyclin A-p27KIP1
3D variability analysis of the hexameric complex. (a,b) Cryo-EM maps representing the (a) closed conformation and (b) open conformation of the hexameric complex as revealed by 3D variability analysis. Cyclin A (purple) bound to p27 (yellow) swings away from N-terminal SKP2 (grey) and SKP1 (green) motif whilst the SKP1 domain concomitantly extends away from the cyclin A-p27 unit. Average distance between SKP1 and cyclin A is ~ 8 Å in closed conformation (as indicated by *) and ~ 16 Å in open conformation (as indicated by **). (c,d) Comparison of the octameric complex PDB 7B5R with the open and closed conformations of the hexameric complex. Superposition of PDB 7B5R (salmon) with the (a) closed conformation (yellow) and (b) open conformation (grey) of the hexameric complex showing that 7B5R falls within the broad conformational space of the hexameric complex. The average distance between SKP1 and cyclin A is ~ 10 Å in PDB 7B5R.
