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. 2021 Aug 5;49(15):8822–8835. doi: 10.1093/nar/gkab677

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — Effects of nucleotides on nsp9 modification. (A) Nucleotide binding to the NiRAN active site. The Mg²⁺ ion is shown as magenta sphere and key NiRAN residues - as sticks. Left, ADP (cyan carbon atoms) from PDB:6XEZ. Right, RDP (lime carbon atoms) modeled in place of ADP; the C1′ cyano group of RDP could clash with the side chain of nsp12 His75. (B) Unlabeled natural NTPs compete with [α³²P]-GTP for transfer to nsp9. (C) GTP analogs and PP_i inhibit NMPylation, but ppGpp and RTP do so less effectively; all nucleotides were present at 0.5 mM. In (B) and (C), NMPylation efficiency was compared to that observed in the absence of competitors, set at 1, and is shown as mean ± SD (n = 3).