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Domain alternation and active site remodeling are conserved structural features of ubiquitin E1
E1 enzymes for ubiquitin (Ub) and Ub-like modifiers (Ubls) harbor two catalytic activities that are required for Ub/Ubl activation: adenylation and thioester bond formation. Structural studies of the E1 for the Ubl small ubiquitin-like modifier (SUMO) revealed a single active site that is transforme...
Uloženo v:
| Vydáno v: | J Biol Chem |
|---|---|
| Hlavní autoři: | , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Biochemistry and Molecular Biology
2017
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5519361/ https://ncbi.nlm.nih.gov/pubmed/28572513 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M117.787622 |
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