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. 2018 Oct 25;9:4441. doi: 10.1038/s41467-018-06953-0

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© The Author(s) 2018

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. 5 — Model of E6-mediated ubiquitylation of p53. Model of E6-mediated ubiquitylation of p53 in the E6AP–E6–p53 enzyme–substrate complex. Upon binding, E6 induces a conformational rearrangement in E6AP that brings the AZUL domain closer to the HECT domain. This leads to the concomitant positioning of E6 and the substrate p53 into the direct vicinity of the catalytic center of E6AP within the enzyme–substrate complex. There, E6 now functions as an adaptor facilitating the direct transfer of ubiquitin from the HECT domain of E6AP to p53