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. 2016 Mar 31;44(10):4957–4967. doi: 10.1093/nar/gkw204

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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-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 3. — BP–dG and replicating base pair in the active site of polκ. (A) The open active site is shown in the back view of the polκ ternary complex (left) and compared to Dpo4 with a flipped-out DNA helix (right, PDB id: 2IA6). Proteins are in a surface representation, and DNA is shown in sticks. Core domains (finger, palm and thumb) are in cyan, N-clasp in beige and little finger (LF) in purple. The BP–dG adduct is in orange with the BPDE rings indicated by arrows. The two enzyme structures are in the same orientation, based on palm domain superposition. (B) Orthogonal views of the replicating base pair, dCTP* (cyan) represents the non-hydrolysable substrate dCMPNPP, BP-dG:dCTP*, in the active site. (C) 2F_o–F_c map contoured at 1σ level over the replicating base pair in polκ–BPG in the same orientations as in (B).