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. 2020 Oct 29;11:5466. doi: 10.1038/s41467-020-19278-8

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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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Fig. 1 — a MORC4 domain architecture. The ATPase and CW domains are colored green and yellow, respectively. The ATPaseCW cassette construct contains aa 29–486 of MORC4 (Q8TE76). b, c Rates of ATP hydrolysis by the ATPase domain of MORC4 (b) and the ATPase-CW cassette of MORC4 (c). Data are represented as mean values +/− S.D. of at least three independent experiments (n ≥ 3). Source data are provided in a Source Data file. d The crystal structure of the dimeric MORC4 ATPase-CW/AMPPNP complex. In protomer A, the ATPase domain and the CW domain are shown in a ribbon diagram and colored green and yellow, respectively. In protomer B, the surface representation of the ATPase domain (white) and the CW domain (yellow) is shown. The magnesium (green) and zinc (gray) atoms are shown as spheres. The AMPPNP molecule is in stick representation. Dashed lines represent residues and loops that are not defined by electron density.