1H, 13C, and 15N backbone and side-chain chemical shift assignment of the toxin Doc in the unbound state.

Steven De Gieter, Remy Loris, Nico Van Nuland, Abel Garcia Pino

Onderzoeksoutput: Articlepeer review

2 Citaten (Scopus)

Samenvatting

Toxin-Antitoxin (TA) modules in bacteria are involved in pathogenesis, antibiotic stress response, persister formation and programmed cell death. The toxin Doc, from the phd/doc module, blocks protein synthesis by targeting the translation machinery. Despite a large wealth of biophysical and biochemical data on the regulatory aspects of the operon transcription and role of Doc co-activator and co-repressor, little is still know on the molecular basis of Doc toxicity. Structural information about this toxin is only available for its inhibited state bound to the antitoxin Phd. Here we report the 1H, 15N and 13C backbone and side chain chemical shift assignments of the toxin Doc from of bacteriophage P1 (the model protein from this family of TA modules) in its free state. The BMRB accession number is 18899.
Originele taal-2English
Pagina's (van-tot)145-148
Aantal pagina's4
TijdschriftBiomol. NMR Assign.
Volume8
StatusPublished - 2014

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  • VIB Seminar 2014

    Steven De Gieter (Participant)

    28 apr 201430 apr 2014

    Activiteit: Participation in workshop, seminar

  • VIB Seminar 2014

    Remy Loris (Keynote speaker)

    28 apr 201430 apr 2014

    Activiteit: Talk or presentation at a workshop/seminar

  • VIB Seminar 2014

    Alexandra Vandervelde (Participant)

    28 apr 201430 apr 2014

    Activiteit: Participation in workshop, seminar

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