Structural basis for UFM1 transfer from UBA5 to UFC1

Ufmylation is a well-established ubiquitin-like protein modification, but its mechanism is largely unclear. Here, the authors present a crystal structure of the ufmylation-specific E1-E2 complex, revealing differences to the ubiquitination machinery and mechanistic details of the ufmylation process.

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Autores principales: Manoj Kumar, Prasanth Padala, Jamal Fahoum, Fouad Hassouna, Tomer Tsaban, Guy Zoltsman, Sayanika Banerjee, Einav Cohen-Kfir, Moshe Dessau, Rina Rosenzweig, Michail N. Isupov, Ora Schueler-Furman, Reuven Wiener
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/92a7bec4aca04541b5ce9c87607504cd
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spelling oai:doaj.org-article:92a7bec4aca04541b5ce9c87607504cd2021-12-02T18:51:37ZStructural basis for UFM1 transfer from UBA5 to UFC110.1038/s41467-021-25994-62041-1723https://doaj.org/article/92a7bec4aca04541b5ce9c87607504cd2021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25994-6https://doaj.org/toc/2041-1723Ufmylation is a well-established ubiquitin-like protein modification, but its mechanism is largely unclear. Here, the authors present a crystal structure of the ufmylation-specific E1-E2 complex, revealing differences to the ubiquitination machinery and mechanistic details of the ufmylation process.Manoj KumarPrasanth PadalaJamal FahoumFouad HassounaTomer TsabanGuy ZoltsmanSayanika BanerjeeEinav Cohen-KfirMoshe DessauRina RosenzweigMichail N. IsupovOra Schueler-FurmanReuven WienerNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Manoj Kumar
Prasanth Padala
Jamal Fahoum
Fouad Hassouna
Tomer Tsaban
Guy Zoltsman
Sayanika Banerjee
Einav Cohen-Kfir
Moshe Dessau
Rina Rosenzweig
Michail N. Isupov
Ora Schueler-Furman
Reuven Wiener
Structural basis for UFM1 transfer from UBA5 to UFC1
description Ufmylation is a well-established ubiquitin-like protein modification, but its mechanism is largely unclear. Here, the authors present a crystal structure of the ufmylation-specific E1-E2 complex, revealing differences to the ubiquitination machinery and mechanistic details of the ufmylation process.
format article
author Manoj Kumar
Prasanth Padala
Jamal Fahoum
Fouad Hassouna
Tomer Tsaban
Guy Zoltsman
Sayanika Banerjee
Einav Cohen-Kfir
Moshe Dessau
Rina Rosenzweig
Michail N. Isupov
Ora Schueler-Furman
Reuven Wiener
author_facet Manoj Kumar
Prasanth Padala
Jamal Fahoum
Fouad Hassouna
Tomer Tsaban
Guy Zoltsman
Sayanika Banerjee
Einav Cohen-Kfir
Moshe Dessau
Rina Rosenzweig
Michail N. Isupov
Ora Schueler-Furman
Reuven Wiener
author_sort Manoj Kumar
title Structural basis for UFM1 transfer from UBA5 to UFC1
title_short Structural basis for UFM1 transfer from UBA5 to UFC1
title_full Structural basis for UFM1 transfer from UBA5 to UFC1
title_fullStr Structural basis for UFM1 transfer from UBA5 to UFC1
title_full_unstemmed Structural basis for UFM1 transfer from UBA5 to UFC1
title_sort structural basis for ufm1 transfer from uba5 to ufc1
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/92a7bec4aca04541b5ce9c87607504cd
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