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. 2021 Jan 5;12:121. doi: 10.1038/s41467-020-20359-x

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© The Author(s) 2021

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 Domain architecture of human p97, Npl4, and Ufd1. Unresolved parts are shown with dotted lines. b Single-particle cryo-EM maps (unsharpened, 0.014 threshold) of human p97 in complex with Npl4/Ufd1. Three conformational states were resolved. The position of Npl4 relative to p97 is illustrated in the cartoons. Unresolved linkers between UBXL and ZF1 are represented by dotted lines. The central pore of the D1 ring in State III is highlighted by an arrowhead. The conserved groove of Npl4 that was found to bind an unfolded ubiquitin in the yeast complex structure¹⁴ was marked by a green band in State III.