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. 2019 Aug 9;10:3626. doi: 10.1038/s41467-019-11518-w

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© The Author(s) 2019

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 — Comparison of amino acid sequence and structure of the yeast Hsp90 isoforms. a Sequence alignment of Hsc82 and Hsp82. The NTD of the isoforms is depicted in blue, the charged linker in gray, the MD in green, and the CTD in orange. The differences in amino acid sequence are highlighted in red. b Hsp82 structure in the closed state (PDB ID: 2CG9²⁰). Sequence differences between Hsp82 and Hsc82 are highlighted in red