Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer

RNF4 is a prototypical single-subunit E3 enzyme that can bind both substrate and ubiquitin-loaded E2. Here, the authors show that the RNF4 N-terminal region, although lacking a defined secondary structure, maintains a compact global conformation to facilitate ubiquitin transfer to the substrate.

Bibliographic Details
Main Authors:	Paul Murphy, Yingqi Xu, Sarah L. Rouse, Ellis G. Jaffray, Anna Plechanovová, Steve J. Matthews, J. Carlos Penedo, Ronald T. Hay
Format:	Article
Language:	English
Published:	Nature Publishing Group 2020-07-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-020-17647-x

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spelling	doaj-c9de74e062a44078a1b0ae8e8b67bf152021-08-01T11:40:07ZengNature Publishing GroupNature Communications2041-17232020-07-0111111310.1038/s41467-020-17647-xFunctional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transferPaul Murphy0Yingqi Xu1Sarah L. Rouse2Ellis G. Jaffray3Anna Plechanovová4Steve J. Matthews5J. Carlos Penedo6Ronald T. Hay7Centre for Gene Regulation and Expression, School of Life Sciences, University of DundeeCentre for Structural Biology, Department of Life Sciences, Imperial College LondonCentre for Structural Biology, Department of Life Sciences, Imperial College LondonCentre for Gene Regulation and Expression, School of Life Sciences, University of DundeeCentre for Gene Regulation and Expression, School of Life Sciences, University of DundeeCentre for Structural Biology, Department of Life Sciences, Imperial College LondonCentre of Biophotonics, School of Physics and Astronomy, University of St. AndrewsCentre for Gene Regulation and Expression, School of Life Sciences, University of DundeeRNF4 is a prototypical single-subunit E3 enzyme that can bind both substrate and ubiquitin-loaded E2. Here, the authors show that the RNF4 N-terminal region, although lacking a defined secondary structure, maintains a compact global conformation to facilitate ubiquitin transfer to the substrate.https://doi.org/10.1038/s41467-020-17647-x
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Paul Murphy Yingqi Xu Sarah L. Rouse Ellis G. Jaffray Anna Plechanovová Steve J. Matthews J. Carlos Penedo Ronald T. Hay
spellingShingle	Paul Murphy Yingqi Xu Sarah L. Rouse Ellis G. Jaffray Anna Plechanovová Steve J. Matthews J. Carlos Penedo Ronald T. Hay Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer Nature Communications
author_facet	Paul Murphy Yingqi Xu Sarah L. Rouse Ellis G. Jaffray Anna Plechanovová Steve J. Matthews J. Carlos Penedo Ronald T. Hay
author_sort	Paul Murphy
title	Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer
title_short	Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer
title_full	Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer
title_fullStr	Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer
title_full_unstemmed	Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer
title_sort	functional 3d architecture in an intrinsically disordered e3 ligase domain facilitates ubiquitin transfer
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2020-07-01
description	RNF4 is a prototypical single-subunit E3 enzyme that can bind both substrate and ubiquitin-loaded E2. Here, the authors show that the RNF4 N-terminal region, although lacking a defined secondary structure, maintains a compact global conformation to facilitate ubiquitin transfer to the substrate.
url	https://doi.org/10.1038/s41467-020-17647-x
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Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer

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