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. 2018 Jul 19;46(15):8010–8022. doi: 10.1093/nar/gky621

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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 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 5. — Conformation of the active site histidines in (6-4) photolyases. (A) Enhanced view of the (6-4)PP interactions with the two prominent residues H357 (His₁) and H361 (His₂) of CraCRY (gray). Distances (in Å) were measured between the histidines, the DNA lesion and two water atoms (red). (B) Comparison of the active site of CraCRY (6FN0, gray) with Dm(6-4) (3CVU, wheat) (r.m.s.d. 0.658 Å). The (6-4)PP bound to Dm(6-4) (red) is slightly tilted compared to the (6-4)PP bound to CraCRY (green).