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. 2019 Jan 21;20:1. doi: 10.1186/s12858-019-0104-5

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© The Author(s). 2019

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 5 — Ypd1-G68Q structure is similar to that of wild-type Ypd1. Overlay of wild-type Ypd1 (cyan) (PDB ID: 1QSP) and the Ypd1-G68Q mutant (magenta). The helices are numbered sequentially A to G from the N terminus to the C terminus, with the four-helix bundle core composed of helices B, C, D and G. The phosphorylatable histidine and H + 4 glycine or glutamine are shown in stick representation. Movement of the αA helix is observed with a RMSD of 1.7 Å for this region. Inset: Electron density for the substituted Q residue at position 68 in Ypd1 as shown by the F_o-F_c omit map (green mesh), contoured at 3.0 σ