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. 2022 Apr 21;29(5):420–429. doi: 10.1038/s41594-022-00755-1

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© The Author(s) 2022

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, A map at 2.5-Å resolution of closed-TRiC in complex with Nb18 in top (left) and side (right) views. b, Cartoon representation of closed TRiC in same views as in a. c, Flattened scheme of subunit arrangement for the two stacked rings. d, Nucleotide-binding site of CCT7 bound with ADP–Mg²⁺–AlF₃. Conserved interacting residues are shown as sticks. e, Side slice of closed-TRiC (fully empty class 4), highlighting the septum at the ring interface that creates two cavities in the TRiC interior. f, Section of the ring interface, viewed from the interior, showing examples of intra-ring (termini–hairpin sheets) and inter-ring (plug–socket, N extensions) contacts.