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. 2017 Jun 27;8:15907. doi: 10.1038/ncomms15907

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Copyright © 2017, The Author(s)

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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Structural alignment of the HsRecQ4 structure (a) with the structures of EcRecQ (PDB 1oyw) (b), HsRecQ1 (PDB 2wwy) (c) and HsBLM (PDB 4o3m) (d). Alignments were created in pymol. All structures were superimposed utilizing the isolated HD2 of HsRecQ4. HsRecQ4 is depicted in gray within each alignment for convenient comparison. Constructs used for crystallization of each RecQ variant are illustrated below the alignment, with the colour code and abbreviations as in Fig. 1a. The alignments demonstrate that the R4ZBD of RecQ4 assumes a unique structural fold, which does not resemble the typical RQC domain of other RecQ helicases. Furthermore, the R4ZBD acquires a unique position within the RecQ4 structure, adjacent to HD1, while all RQC domains are consistently located adjacent to the HD2. The two DNA-complex structures (c,d) depict a RecQ-conserved mode of DNA binding, with the ssDNA bound across the ATPase domain and the dsDNA portion bound via the WH domain. (Note: The HsBLM structure (4o3m) also features the HRDC domain, which was omitted for the purpose of a uniform comparison).