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. 2019 Oct 11;47(20):10830–10841. doi: 10.1093/nar/gkz866

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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. — Structures of wild-type I-OnuI with cognate A+3 and A+3G substrates. In all panels, the I-OnuI protein is colored according to substrate, with A+3 as yellow and A+3G as green. Note that the I-OnuI/A+G3 complex is post-cleavage and both DNA strands are cut. (A) Schematic of substrates used in crystallization experiment. (B) The network of direct and water-mediated contacts between K227, W234, D236 and bases +3, +4 and +5. (C) Distortions in the phosphate backbone of the A+3G substrate relative to the cognate substrate. (D) Perturbations of the active site residues E178 and E22 of the A+3G substrate relative to the cognate substrate. All panels are stereo images.