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. 2018 Oct 24;46(22):12166–12176. doi: 10.1093/nar/gky970

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© The Author(s) 2018. 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 5. — Active site structure of mTREX2–product complex. (A) The superposition of the two active sites in mTREX2–substrate complex (mTREX2-Y-shaped DNA complex) and mTREX2–product complex. The substrate complex is colored pink. The scissile phosphates are displayed as pink or orange balls and labeled ‘P’. The water molecules and two Mg²⁺ are displayed as light blue and blue balls, respectively. (B) Structural model of the transition state is between substrate cleaving and product releasing. mTREX2 protein is displayed as surface mode.