Fig. 6: Structural rearrangement of E6AP upon binding with E6.

a, b Side (a) and top (b) views of the docking of the E6AP model from E6AP/E6 complex in Att1 into the density map of the E6AP monomer. N-terminal region (NTR), N-lobe and C-lobe of E6AP are yellow, green, and red, respectively. c RMSF profiles for each residue of E6AP over the 500-ns simulation for each of the three systems containing the dimer of the E6AP/E6 protomer (red), one E6AP/E6 protomer (blue), and the isolated E6AP (as extracted from the E6AP/E6 complex, black). Flexible regions are highlighted, which are inside the loop-helix-loop element (residues 398-418, red box) and the α1-helix (residues 503-514, green box). d Alignment of the E6AP snapshot structures during the 500-ns simulation for the three systems. The initial structure (0 ns) and the snapshot structures at 100, 300, and 500 ns are colored in gray, yellow, red, and blue, respectively. e A working model showing the hijacking activity of the E6AP ubiquitin ligase by HPV E6 to ubiquitinate p53. The red arrows indicate the proximity of the C-lobe of E6AP to E2 or to substrates when two E6AP/E6 protomers sway around the crossed region of the two extended α1-helices. The short α1-helix of the E6AP monomer is shown in grey. The extended parts of the long α1-helix in the E6AP/E6 are shown in blue. Source data are provided as a Source Data file.