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. 2022 Dec 22;51(1):475–487. doi: 10.1093/nar/gkac1207

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© The Author(s) 2022. 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 (https://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 7. — Evaluation of NSP14 as part of the Cap(0)RTC complex. (A) Overview of the positioning of NSP14 within the monomeric Cap(0)RTC complex based on the recently published Cryo EM structure(14). Subunits are colored individually as labeled with NSP14 and NSP10 shown in the cartoon format. (B) Overview of the positioning of NSP14 within the Dimeric Cap(0)RTC complex as viewed along the two-fold symmetry axis. (C) Overlay of NSP14 alone with the NSP14 NSP10 complex within the Cap(0)RTC complex. The N-terminal region of NSP14 forms significant steric clashes with NSP9. (D) Overlay of the NSP14-NSP10-RNA complex (7N0B)(9) onto the Cap(0)RTC complex. Severe steric clashes are evident with the RNA substrate (shown in black in stick format) suggesting this arrangement is not compatible with nuclease activity.