1H, 13C, and 15N backbone and side-chain chemical shift assignment of the toxin Doc in the unbound state
- 199 Downloads
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.
KeywordsToxin–antitoxin module Macromolecular complex NMR Doc Bacteriophage P1
This work received financial support from the VIB, FWO-Vlaanderen, the Onderzoeksfonds of the Vrije Universiteit Brussel (OZR-VUB) and the Hercules Foundation. A.G.P. is a post-doctoral fellow of the FWO-Vlaanderen.
- Arbing MA, Handelman SK, Kuzin AP, Verdon G, Wang C, Su M, Rothenbacher FP, Abashidze M, Liu M, Hurley JM et al (2010) Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin–antitoxin systems. Structure 18:996–1010CrossRefGoogle Scholar
- Johnson BA (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 278:313–352Google Scholar