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. 2022 Apr 27;8(17):eabm2827. doi: 10.1126/sciadv.abm2827

Fig. 3. Unique features of EBV BORF2 and its interaction with A3B.

Fig. 3.

(A) Overlay of the structures of BORF2 (blue), human RNR α subunit (PDB: 6aui, chain A; tan), and E. coli RNR α subunit (PDB: 6w4x, chain B; green). Novel BORF2 insertions SHI and LLI are depicted in red. Loop regions surrounding the A3Bctd active site are labeled L1, L3, and L7. (B) Schematic of BORF2 (1 to 826 amino acids) showing the A3B interacting regions (orange) and the novel SHI and LLI insertions (red). Bottom left: Structural comparison of the BORF2 SHI and the corresponding regions of human and E. coli RNR α subunits. Bottom right: Cryo-EM map of the BORF2 SHI domain in blue. (C) Close-up of BORF2-A3B interface showing a network of interactions. BORF2 is depicted in blue, BORF2 SHI is in red, and A3Bctd is in orange, with ribbon and surface representations (top and bottom, respectively). (D) Co-IP reactions with the indicated BORF2 constructs (anti-FLAG) and A3Bctd-eGFP. A parallel reaction with BORF2 and A3Gctd-eGFP is shown as an additional negative control. Input blots are shown below including anti-tubulin as a loading control.