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. 2023 Nov 13;14:7340. doi: 10.1038/s41467-023-43035-2

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© The Author(s) 2023

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a, b Structures of the overlapping long helices (LH), which connects the NGD and AAA+ domains of the protomers Ob1, Ob3, and Ob5, in the substrate-free pentamer (a) and in the substrate-bound close-ring hexamer (b), which are aligned based on the AAA3 domain. The substrate (S) is shown in surface representation and colored in magenta. The Ac2/4 protomers are omitted for clarity. c The protomers Ob1, Ob3, and Ob5 in the substrate (S)-free and S-bound states are superimposed based on the AAA+ domain (residues 297–490). Only residues 1–490 are shown.