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

Title(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignment of the toxin Doc in the unbound state.
Publication TypeJournal Article
Year of Publication2013
AuthorsDe Gieter, S., R. Loris, N. A. J. van Nuland, and A. Garcia-Pino
JournalBiomol NMR Assign
Date Published2013 Feb 19
Type of Articleta
ISSN1874-270X
Abstract

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 (1)H, (15)N and (13)C 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.

DOI10.1007/s12104-013-9471-9
Alternate JournalBiomol NMR Assign
PubMed ID23420131
subject_category: 
Research group: