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. 2021 Sep 6;12:5254. doi: 10.1038/s41467-021-25574-8

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© The Author(s) 2021

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 Depicted here is the cryo-EM map of Pdr5 in inward-open conformation (ADP-Pdr5). The map is coloured according to the domain organisation (see key). The grey transparent envelope surrounding the protein is a Gaussian-filtered (2σ) version of the same map, showing the extent and shape of the peptidisc shell around Pdr5. b Atomic model of Pdr5 built and refined against the map, in cartoon representation. c Top view (cytoplasmic side) of the nucleotide-binding domains of Pdr5, showing the position of the bound nucleotides. The linker domain is also depicted. d Side and top views of the transmembrane domain of Pdr5 with α-helices shown schematically as cylinders and numbered sequentially (TH1a–12) from the N-terminus (cf. Supplementary Fig. 5 and S6). This panel also includes the linker domain and its two helices H3 and H17. e, f Two portions of the ADP-Pdr5 cryo-EM map, showing the reconstructed volume around representative secondary structural features: e α-helices TH7b and TH8 of TMD1 domain and (f) a β-sheet in NBD1 domain. Arrowheads point to amino acid residues that have been arbitrarily chosen for orientation purposes. Abbreviations: ECD, extracellular domain; LD, linker domain; NBD, nucleotide-binding domain; TMD, transmembrane domain.