A MUB E2 structure reveals E1 selectivity between cognate ubiquitin E2s in eukaryotes
Regulators of the important ubiquitylation cascade are not well studied. Here, the authors report the crystal structure of a prenylated membrane-anchored ubiquitin-fold protein from Arabidopsisbound to an E2 protein and conclude that it is an example of selective activation between E2 enzymes.
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| Autores principales: | , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2016
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/ba8ab800ee01437e95b50a46ccc7136a |
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| Sumario: | Regulators of the important ubiquitylation cascade are not well studied. Here, the authors report the crystal structure of a prenylated membrane-anchored ubiquitin-fold protein from Arabidopsisbound to an E2 protein and conclude that it is an example of selective activation between E2 enzymes. |
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