Fig. 1: Overall structure of the E6AP/E6 complex. | Nature Communications

Fig. 1: Overall structure of the E6AP/E6 complex.

From: Structural insights into the functional mechanism of the ubiquitin ligase E6AP

Fig. 1

a, b Side view (a) and top view (b) of the density map of the E6AP/E6 complex. The E6AP/E6 complex is a dimer of the E6AP/E6 protomer in the attached-1 (Att1) state. E6AP and E6 are green and red, respectively, in protomer 1 and yellow and purple, respectively, in protomer 2. Maps were processed using DeepEMhancer. c Atomic model of the E6AP/E6 complex. The view and colors are same as that in a. d Structural architecture of E6AP in the E6AP/E6 complex. E6AP presents as a tower standing on a base. The tower is exclusively produced from the N-terminal region (NTR, yellow) of E6AP, whereas the base is formed by contributions from the C-terminal HECT domain (green N-lobe and red C-lobe), the N-helix, and the loop-helix-loop element. Note that the structural features presented here are based on the conformation of the E6AP/E6 complex in the Att1 state. e Structural characteristics of E6 in the E6AP/E6 complex in the Att1 state. E6 contains an E6N domain, an E6C zinc-binding domain, and a linker helix tethering E6N to E6C. f Two 3-helix bundles at the interface between two E6AP/E6 protomers in Att1 state. The small cartoon in the lower left corner is shown for orientation purposes and indicates a close-up view enclosed by the black line. E6AP and E6 are colored as in b. g Zoomed-in view of the regions outlined by the red line.

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