Extended Data Fig. 8: The active site of the RdRp domain. | Nature Microbiology

Extended Data Fig. 8: The active site of the RdRp domain.

From: Structure of severe fever with thrombocytopenia syndrome virus L protein elucidates the mechanisms of viral transcription initiation

Extended Data Fig. 8

a, The details of the RdRp motifs of SFTSV-L. This figure is generally the same as Fig. 5a, with one exception that the cation, assumed to be a magnesium ion, is shown as a red sphere. In contrast, two catalytic manganese ions from the polio virus elongation complex structure4 are shown as black spheres. b, The bound cation and surrounding residues are covered by cryo-EM densities. The bonds formed between SFTSV-L polypeptide and the cation are labeled with distance. c, The electrostatic surface potential of SFTSV-L RdRp tunnels. The positive surface is colored blue, the negative surface, red, with limits ±70 kbT/ec. The regions belong to the NTP entry, template entry, template exit and product exit tunnles are indicated out by dashed lines. d, The entrance of NTP entry tunnel, and e, the entrance of template entry tunnel. Colors are as in Fig. 4. Superposition of LACV-L 1750 (5AMR) structure shows the position of the 5' vRNA (gray cartoon) in (b). The approximate positions of NTP and template entry tunnels are bordered by dashed lines.

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