Figure 2 | Cell Research

Figure 2

From: Cryo-EM structure and biochemical analysis reveal the basis of the functional difference between human PI3KC3-C1 and -C2

Figure 2

Atomic model building and analysis of C1 and C2. (A, C) The chimeric EM volume of C1 docked with the built atomic model (VPS34-CTD excluded). Within the atomic model, the Beclin1, ATG14L, VPS34 and P150 protein subunits are colored orange, light green, hot pink and cyan, respectively. The chimeric EM volume is presented as a translucent grey surface. A shows the top view and C represents the side view. (B, D) The refined EM volume of C2 docked with the hypothetical atomic model of C2 (VPS34-CTD excluded), which was directly extracted from the model of yeast PI3K complex 2 (PDB code: 5DFZ). Within the atomic model, the Beclin1, UVRAG, VPS34 and P150 subunits are colored orange, light green, hot pink and cyan, respectively. The chimeric EM volume is presented as a translucent grey surface. B shows the top view and D represents the side view. The dashed circle in D indicates the electron density from the β-barrel insertion within the NTD of UVRAG. (E, F) The built atomic model of C1 and the docked model of C2. The dashed rectangles indicate Beclin1, ATG14L and the P150 WD domain in C1 and Beclin1, UVRAG and the P150 WD domain in C2, which were extracted from the overall model and are presented in the bottom panels with the same orientation. The relative orientation of these two extracted parts is marked with the rotation axis and angle. The top right panels in E and F show cartoon models of the side and top views of C1 and C2. The green shapes indicate the Beclin1/ATG14L subunits in C1 and the Beclin1/UVRAG subunits in C2. The blue shapes indicate the P150/VPS34-NTD subunits in both complexes.

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