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.

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Autores principales:	Paul Murphy, Yingqi Xu, Sarah L. Rouse, Ellis G. Jaffray, Anna Plechanovová, Steve J. Matthews, J. Carlos Penedo, Ronald T. Hay
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c9de74e062a44078a1b0ae8e8b67bf15
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spelling	oai:doaj.org-article:c9de74e062a44078a1b0ae8e8b67bf152021-12-02T16:31:49ZFunctional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer10.1038/s41467-020-17647-x2041-1723https://doaj.org/article/c9de74e062a44078a1b0ae8e8b67bf152020-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17647-xhttps://doaj.org/toc/2041-1723RNF4 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.Paul MurphyYingqi XuSarah L. RouseEllis G. JaffrayAnna PlechanovováSteve J. MatthewsJ. Carlos PenedoRonald T. HayNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
author	Paul Murphy Yingqi Xu Sarah L. Rouse Ellis G. Jaffray Anna Plechanovová Steve J. Matthews J. Carlos Penedo Ronald T. Hay
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 Portfolio
publishDate	2020
url	https://doaj.org/article/c9de74e062a44078a1b0ae8e8b67bf15
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Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer

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