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. 2019 Sep 23;47(20):10693–10705. doi: 10.1093/nar/gkz792

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© The Author(s) 2019. 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 Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 2. — Structural mechanism of rCTP and dCTP incorporation by MsDpo4-WT. (A) The structures of MsDpo4-WT_DNA(dG):dCTP (colored yellow) and MsDpo4-WT_DNA(dG):rCTP (colored violet) superimpose with an RMSD of 0.36 Å. The enzyme structure is shown in cartoon representation, DNA is shown as ribbons, and the incoming nucleotide and the Leu14 residue (in green) are shown in stick representation. A close-up of the region surrounding the incoming nucleotide, is displayed for (B) MsDpo4_DNA(dG):rCTP and (C) MsDpo4_DNA(dG):dCTP. The comparison shows that the dCTP and rCTP bind the MsDpo4 active site in the same location and conformation with marginal differences in the enzyme structure.