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. 2016 Jul 15;44(21):10423–10436. doi: 10.1093/nar/gkw637

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© The Author(s) 2016. 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 7. — Comparision of RNMT–RAM structure with Vaccinia virus D1 cap methyltransferase and its activating subunit D12. RNMT and D1 are shown in cyan, whereas RAM and D12 in magenta. The RNMT hinge and the hinge-like region in D1 comprising of helices αG and αH are highlighted in green. D1 lacks a region with structural similarity to the RNMT lobe, which is shown in orange. The zoomed images demarcate active site residues within helix A and αZ of RNMT and D1 respectively. Residues involved in a polar interaction (dashed line) critical for the stability of helix A in RNMT and the corresponding residues in D1 have also been highlighted as sticks.

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