Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex

Carolin Sailer; Fabian Offensperger; Alexandra Julier; Kai-Michael Kammer; Ryan Walker-Gray; Matthew G. Gold; Martin Scheffner; Florian Stengel

doi:10.1038/s41467-018-06953-0

Nature Communications (Oct 2018)

Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex

Carolin Sailer,
Fabian Offensperger,
Alexandra Julier,
Kai-Michael Kammer,
Ryan Walker-Gray,
Matthew G. Gold,
Martin Scheffner,
Florian Stengel

Affiliations

Carolin Sailer: Department of Biology, University of Konstanz
Fabian Offensperger: Department of Biology, University of Konstanz
Alexandra Julier: Department of Biology, University of Konstanz
Kai-Michael Kammer: Department of Biology, University of Konstanz
Ryan Walker-Gray: Department of Neuroscience, Physiology & Pharmacology, University College London
Matthew G. Gold: Department of Neuroscience, Physiology & Pharmacology, University College London
Martin Scheffner: Department of Biology, University of Konstanz
Florian Stengel: Department of Biology, University of Konstanz

DOI: https://doi.org/10.1038/s41467-018-06953-0
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 12

Abstract

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Oncoprotein E6 facilitates the E6AP-catalyzed ubiquitination of p53. Here, the authors study the structural basis of this process by qualitative and quantitative cross-linking mass spectrometry, providing insights into E6AP-E6-p53 complex assembly and the conformational dynamics that enable p53 ubiquitination.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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