The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

@inproceedings{CastroRoa2013TheFP,
  title={The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu},
  author={Daniel Castro-Roa and Abel Garcia-Pino and Steven De Gieter and Nico A. J. van Nuland and Remy Loris and Nikolay Zenkin},
  booktitle={Nature chemical biology},
  year={2013}
}
Fic proteins are ubiquitous in all of the domains of life and have critical roles in multiple cellular processes through AMPylation of (transfer of AMP to) target proteins. Doc from the doc-phd toxin-antitoxin module is a member of the Fic family and inhibits bacterial translation by an unknown mechanism. Here we show that, in contrast to having AMPylating activity, Doc is a new type of kinase that inhibits bacterial translation by phosphorylating the conserved threonine (Thr382) of the… CONTINUE READING
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1)H, (13)C, and (15)N backbone and sidechain chemical shift assignment of the toxin

S De Gieter, R Loris, NA van Nuland, A. Garcia-Pino
Doc in the unbound state. Biomol NMR Assign • 2013

Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNA.

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