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

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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Bibliographic Details
Main Authors: Priyesh Mohanty, Rashmi Agrata, Batul Ismail Habibullah, Arun G S, Ranabir Das
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2019-10-01
Series:eLife
Subjects:
deamidation
ubiquitination
Shigella
transient complex
NMR spectroscopy
MD simulations
Online Access:https://elifesciences.org/articles/49223

Internet

https://elifesciences.org/articles/49223

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