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. 2024 Apr 12;31(7):1134–1144. doi: 10.1038/s41594-024-01281-y

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© The Author(s) 2024

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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Extended Data Fig. 4 — a, Electrostatic surface potential of Spc98 and Spc97 in the γTuSC structure shows that the coiled-coil protein is lined against a positively charged patch on Spc98^GRIP2. b, Alphafold2 predictions and cryo-EM density insets of the interface between the γ-tubulin^CTR and Spc98^GRIP2 (top panel) and Spc97^GRIP2 (lower panel). The γ-tubulin^CTR is predicted to bind extensively along the Spc98^GRIP2 domain and extends beyond the conserved ‘DSYL’ motif towards the coiled-coil density. At the Spc97^GRIP2 domain on the other hand, the γ-tubulin^CTR tail is not predicted to interact beyond the ‘DSYL’ motif. c, γ-tubulin pLDDT scores mapped on the Alphafold2 predictions shown in panel b. γ-tubulin is coloured by the pLDDT score while Spc98 and Spc97 are coloured by subunit. PAE plots for the best model are also shown as insets. d, The unstructured γ-tubulin^CTR extends toward the coiled-coil density in the γTuRC average.