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. 2022 May 25;15(6):659. doi: 10.3390/ph15060659

Figure 2.

Figure 2

The predicted RVFV-L RdRp active site. (A) The RVFV-L RdRp core (residues 769–1358) is highlighted in green with conserved RNA synthesis chamber (active site), organized by conserved structural motifs in distinct colors. The four predicted tunnels are marked with arrows as an entrance (template and NTP entry) into the active site chamber and exit tunnels (template and product exit). The arrangement of structurally conserved RdRp motifs are colored magenta, red, golden, khaki, brown, purple, and cyan for motifs A–F, respectively, and superimposed on SFTSV-L RdRp core (light orange). (B) The predicted binding site residues are aligned and highlighted through multiple structure alignment (MSA) in representative motifs. These conserved residues are highlighted in stick representation accordingly. Superposition of the poliovirus elongation complex structure (PDB ID: 3OL8) and foot-and-mouth disease virus in complex with RTP (PDB ID: 2E9R) displays the conformation of RTP (yellow) and positions of the catalytic divalent cations (black spheres). Viral names in MSA are abbreviated as follows: Influenza A (FluA), B (FluB), and C (FluC) virus polymerase, Rift valley fever virus (RVFV), and Severe fever with thrombocytopenia syndrome virus (SFTSV).