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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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Extended Data Fig. 8 — For all panels, tubulin is coloured by domain: N-terminal domain (blue), TBD (crimson), and C-terminal domain (dark green). Green dashes indicate van der Waals contacts; blue dashes indicate hydrogen bonds. TRiC structural features labelled are apical domain loop (AL), stem-loop (SL), C-terminus (CT) and helix X (αX). (a) CCT8 interacts with tubulin N-terminus (Arg2, Glu53, Asp74) using its stem-loop (His59, Leu60) and intermediate domain (Arg314, Asn316). (b) CCT6 contacts tubulin N-terminal α4 (Glu125) and α5 (Glu157, Glu158, Tyr159) through a β-sheet of the apical domain. Additionally, CCT6 stem-loop (Ala51) and C-terminus (Met526) interact with tubulin N- and C-termini, along with CCT3 stem-loop (Met54). (c) Tubulin C-terminus (Phe402, Trp405) interacts with CCT3 stem-loop, helix α3 from equatorial domain (Glu89), and intermediate domain. (d) CCT1 apical domain loop (Lys245) and stem-loop (Asp358) form few tubulin contacts (Phe260, Pro261), involving also CCT3 apical domain loop and helix α3.