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. 2019 Aug 10;47(17):9448–9463. doi: 10.1093/nar/gkz703

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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 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. — Helical domain orients DNA binding in Class 2 OLD nucleases. (A) Electrostatic surface of Bp^CTR with modeled DNA (G:T mismatched substrate taken from PDB: 3K0S). Electrostatic potential calculated with APBS (37). Scale indicates coloring of the potential from –3K_bT/e_c to +3K_bT/e_c. The four basic patches around the active site cleft are numbered in yellow. (B) Side and end views of Toprim family superposition with modeled DNA substrate bound to Bp OLD^CTR. Toprim cores are colored white with Inserts 1–5 individually labeled. Bp Toprim and helical domains are colored purple and yellow respectively. (C) Arrangement of Bp^CTR active site with modeled DNA. (D) Proposed two-metal catalysis mechanism for Class 2 OLD nuclease cleavage.