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. 2020 Feb 25;11:1038. doi: 10.1038/s41467-020-14842-8

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© The Author(s) 2020

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. 2 — a Superposition of MTBD-Low (cyan) and mouse MTBD SRS chimera (PDB code 3EER, light green) viewed from the side. b Superposition of MTBD-High (pink) and MTBD-Low (cyan). c Superposition of cryo-EM model of MTBD in complex with MTs in the DTT(−) (orange) and DTT(+) (magenta) conditions. d The superposition of MTBD-Low (cyan), MTBD-High (pink), and MTBD-Bound (magenta). Only the CC1, H1, and CC2 moieties are colored. The Cα positions of CC1 and CC2 residues that signify the coiled-coil registry are shown by spheres. The notable conformational changes of H1 and CC1 are indicated by pink arrows. e, f Superposition of the cryo-EM map filtered to 4 Å and the model of MTBD in complex with MTs in (e) DTT(−) (yellow) and in (f) DTT(+) (magenta) conditions. Asterisks (*) are placed on the regions corresponding to the hydrophobic interactions between CC1 and CC2 in both maps.