FIGURE 7.

ATP appears to be exploited by SARS‐CoV‐2 to promote its life cycle. (a) Domain organization of SARS‐CoV‐2 nucleocapsid (N) protein composed of the N‐terminal domain (NTD) for RNA‐binding and C‐terminal domain (CTD) for dimerization, as well as three intrinsically disordered regions (IDRs). (b) Turbidity curves of N protein at 20 μM without (red circles) and with the pre‐existence of A24 at 1:0.5 (blue circles) upon addition of ATP at different ratios. (c) DIC images of N protein in the presence of ATP at different ratios. (d) The lowest‐energy docking model of the ATP‐RBD complex with ATP in ball‐and‐stick, and RBD in ribbon or in electrostatic potential surface. (e) A proposed scheme to illustrate that ATP might be hijacked by SARS‐CoV‐2 to promote its life cycle by facilitating the initial uncoating of the gRNA‐Nprotein condensate and subsequent localizing to replicase‐transcriptase complex