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. 2018 Feb 1;8:2127. doi: 10.1038/s41598-018-20557-0

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© The Author(s) 2018

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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Crystal structures of TTERecF and TTERecF-ATP. (A) Cartoon representation of TTERecF. β-strands are numbered and α-helixes are lettered. The labels for domains I and II are indicated on the left. (B) Cartoon representations of the Rad50 (PDB:3QF7) and SMC protein (PDB:3ZGX) are shown in purple and salmon, respectively; the labels for lobes I and II are indicated in the middle. (C) The substrate ATP binds to TTERecF; TTERecF is shown as cartoon and the substrate is represented by sticks. Domains I and II are shown in pink and light blue, respectively, in the TTERecF A molecule, but green and yellow, respectively, in the TTERecF B molecule. The Walker A motif, Walker B motif, and the signature motif in the active site are shown in red. The 2F_O- F_C electron density for ATP contoured at the 1.0σ level is shown as blue mesh. (D) Electrostatic properties of TTERecF and sliced surface view of the ATP binding tunnel. The complexes are shown as solvent-accessible surfaces coloured by electrostatic potential (red, acidic; blue, basic).