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. 2020 Jan 15;10:393. doi: 10.1038/s41598-019-56825-w

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Overall structure of the fowl poxvirus resolvase (Fpr). (A) Structure of Fpr with the secondary structure elements labeled. (B) Superposition of Fpr and Cpr monomers based on the central five β-strands. (C) Superposition of Fpr and RuvC from T. thermophiles (TthRuvC) monomers, highlighting that two proteins have different αC and αD helices (colored differently from the rest of the monomers and indicated by arrows). αB and the preceding loop in TthRuvC are longer than the counterparts in Fpr, while αC in Fpr superposes onto αD of TthRuvC but is much longer. (D) 90° rotation of C around a horizontal axis. (E,F) Superposition of Fpr and RuvC dimers showing the different shape of Fpr and TthRuvC, F is 90° rotation of E around a vertical axis. (F) Electrostatic surface representation of the Fpr dimer. The negative surface (in red) formed by the active site residues can be seen at the bottom of the DNA binding grooves. The αC helices are shown in magenta. (H) 90° rotation of G around a vertical axis, showing strong positive potentials (blue) on the side of active site of the Fpr dimer. The orientations of G and H are same as E and F respectively.