Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification

The molecular mechanism of ubiquitin transfer from E1 to E2 enzymes is still unclear. By solving the crystal structure of a covalently trapped E1–E2–ubiquitin thioester mimetic, the authors identify two conformations of this complex which suggest an affinity switch mechanism for thioester transfer....

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Autores principales:	Lingmin Yuan, Zongyang Lv, Melanie J. Adams, Shaun K. Olsen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e2f5ddd2897446a6b0118fb160ffec7e
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spelling	oai:doaj.org-article:e2f5ddd2897446a6b0118fb160ffec7e2021-12-02T16:45:10ZCrystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification10.1038/s41467-021-22598-y2041-1723https://doaj.org/article/e2f5ddd2897446a6b0118fb160ffec7e2021-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22598-yhttps://doaj.org/toc/2041-1723The molecular mechanism of ubiquitin transfer from E1 to E2 enzymes is still unclear. By solving the crystal structure of a covalently trapped E1–E2–ubiquitin thioester mimetic, the authors identify two conformations of this complex which suggest an affinity switch mechanism for thioester transfer.Lingmin YuanZongyang LvMelanie J. AdamsShaun K. OlsenNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Lingmin Yuan Zongyang Lv Melanie J. Adams Shaun K. Olsen Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification
description	The molecular mechanism of ubiquitin transfer from E1 to E2 enzymes is still unclear. By solving the crystal structure of a covalently trapped E1–E2–ubiquitin thioester mimetic, the authors identify two conformations of this complex which suggest an affinity switch mechanism for thioester transfer.
format	article
author	Lingmin Yuan Zongyang Lv Melanie J. Adams Shaun K. Olsen
author_facet	Lingmin Yuan Zongyang Lv Melanie J. Adams Shaun K. Olsen
author_sort	Lingmin Yuan
title	Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification
title_short	Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification
title_full	Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification
title_fullStr	Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification
title_full_unstemmed	Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification
title_sort	crystal structures of an e1–e2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/e2f5ddd2897446a6b0118fb160ffec7e
work_keys_str_mv	AT lingminyuan crystalstructuresofane1e2ubiquitinthioestermimeticrevealmolecularmechanismsoftransthioesterification AT zongyanglv crystalstructuresofane1e2ubiquitinthioestermimeticrevealmolecularmechanismsoftransthioesterification AT melaniejadams crystalstructuresofane1e2ubiquitinthioestermimeticrevealmolecularmechanismsoftransthioesterification AT shaunkolsen crystalstructuresofane1e2ubiquitinthioestermimeticrevealmolecularmechanismsoftransthioesterification
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Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification

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