Deamidation disrupts native and transient contacts to weaken the interaction between UBC13 and RING-finger E3 ligases

The deamidase OspI from enteric bacteria Shigella flexneri deamidates a glutamine residue in the host ubiquitin-conjugating enzyme UBC13 and converts it to glutamate (Q100E). Consequently, its polyubiquitination activity in complex with the RING-finger ubiquitin ligase TRAF6 and the downstream NF-κB...

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Detalles Bibliográficos
Autores principales: Mohanty, Priyesh, Agrata, Rashmi, Habibullah, Batul Ismail, G S, Arun, Das, Ranabir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2019
Materias:
Biochemistry and Chemical Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6874479/
https://www.ncbi.nlm.nih.gov/pubmed/31638574
http://dx.doi.org/10.7554/eLife.49223

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6874479/
https://www.ncbi.nlm.nih.gov/pubmed/31638574
http://dx.doi.org/10.7554/eLife.49223

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