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. Author manuscript; available in PMC: 2018 Jul 5.
Published in final edited form as: Biochemistry. 2018 Apr 12;57(16):2325–2334. doi: 10.1021/acs.biochem.8b00357

Figure 1.

Figure 1

Structure of the octahedral core of the human E2p IC domain solved by cryoEM single particle reconstruction. (A) CryoEM 3D reconstruction of the dodecahedral core of human E2p IC domain. Radially colored surface view is shown along the 5-, 3-, and 2-fold axes from left to right. The 2-fold view (right) is cut through to show the interior. (B) Rainbow-colored ribbon of the atomic model of the human E2p IC domain (left) and superimposition of the IC domains (right) of human E2p, A. vinelandii E2p (PDB ID: 1EAA), E. coli E2o (PDB ID: 1E2O), and bovine E2b (PDB ID: 2IHW). The left and right panels are in the same angle of view. The regions with high variability among these structures are highlighted with dashed boxes in the superimposition. The resolvable N-terminal residues are indicated by diamond (human E2p, E. coli E2o, and bovine E2b) or asterisk (A. vinelandii E2p). The inset in the middle shows the extended “tip” in the human E2p IC trimers formed by the loop connecting βI2 and βJ. (C) Structure of the human E2p IC trimer with the subunits colored in different shades of blue. (D) Close-up views of the interface between two subunits within a trimer of the IC domain. The subunits are colored in different shades of blue as in (C), and the prime symbol is used for the 3-fold related subunit on the clockwise position.