CORD-19:fed42d29b5f366d5fd3076e37cc781e6b68450ce JSONTXT 7 Projects

Supplementary Materials Abstract Structural comparisons of (A) methylated nsp10 (magenta), nsp10 (cyan), and truncated nsp10 (green) and (B) PRRSV nsp10 (cyan) and EAV nsp10 (green). A 45° rotation view is shown in the right panel. The structures are superimposed on 1A domains. ATPase activities of (A) PRRSV nsp10 and (B) EAV nsp10 were determined from Lineweaver-Burk plots of hydrolysis activity using the malachite green assay. Error bars represent SD values from three separate experiments. Structural characterization of the PRRSV nsp10 ZBD. (A) Structure of the cross-braced zinc finger and (B) treble-clef zinc finger. The residues coordinating the Zn 2+ ions are shown as sticks. (C) Superposition of the ZBD of PRRSV nsp10 (green) and EAV nsp10 (PDB code: 4N0N; grey). (D) Sequence alignment of ZBD of PRRSV nsp10 and EAV nsp10. Multiple sequence alignment was carried out using Clustal Omega [1] . The illustration of sequence alignment was generated using ALINE [2] . Minor manual adjustments were performed in accordance with the superimposition. Putative protein interaction surface of the nsp10 ZBD. Hydrophobic surface of (A) the PRRSV nsp10 ZBD and (C) the EAV nsp10 ZBD. The hydrophobic pocket is covered by domain 1B in PRRSV nsp10. A 45° rotation view is shown in the right panel. Close-up view of hydrophobic pockets of (B) PRRSV nsp10 and (D) EAV nsp10. Domain 1B is omitted for clarity. Hydrophobic residues are shown as sticks. The orientation is the same as in panels A and C. Colors are calculated according to the method (https://pymolwiki.org/index.php/ Color_h).