title: ¹H, ¹³C, and ¹⁵N backbone and side-chain chemical shift assignment of the toxin Doc in the unbound state.
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.
authors: Jean Jeener NMR Centre, Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussel, Belgium.
authors: Steven
authors: S
authors: De Gieter
authors: Remy
authors: R
authors: Loris
authors: Nico A J
authors: NA
authors: van Nuland
authors: Abel
authors: A
authors: Garcia-Pino
mesh_terms: D000595:Amino Acid Sequence; D017101:Bacteriophage P1 / Q000378:metabolism*; D002247:Carbon Isotopes; D006859:Hydrogen; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D002247:Carbon Isotopes; C083664:Doc protein, Enterobacteria phage P1; D009587:Nitrogen Isotopes; D014764:Viral Proteins; D006859:Hydrogen