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. 2017 Mar 30;8:14860. doi: 10.1038/ncomms14860

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Copyright © 2017, The Author(s)

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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(a–c) Structures of AUF and RAPTA-T adduct sites. H2A, H2B, H3 and H4 histone proteins are shown respectively with yellow, salmon, cyan and green backbone colouring. (a) Overview of AUF and RAPTA-T binding, illustrating the ≥27 Å separation of the two types of adducts. The arrow indicates the pseudo-twofold symmetry axis of the nucleosome. (b) Structure of the AUF-histone adducts. Dashed lines indicate hydrogen bonding with the H3 H113 imidazole epsilon nitrogen groups. (c) The van der Waals environment of an AUF adduct, shown in space-filling representation. (d) Superposition of the native NCP (magenta), RAPTA-T–NCP (yellow) and RAPTA-T/AUF–NCP (cyan) models, illustrating that the structures of the RAPTA-T-containing models are nearly identical, whereas that of the native NCP differs subtly in the vicinity of where the adducts form.