Title | (1)H, (13)C, and (15)N backbone and side-chain chemical shift assignment of the toxin Doc in the unbound state. |
Publication Type | Journal Article |
Year of Publication | 2013 |
Authors | De Gieter, S., R. Loris, N. A. J. van Nuland, and A. Garcia-Pino |
Journal | Biomol NMR Assign |
Date Published | 2013 Feb 19 |
Type of Article | ta |
ISSN | 1874-270X |
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. |
DOI | 10.1007/s12104-013-9471-9 |
Alternate Journal | Biomol NMR Assign |
PubMed ID | 23420131 |
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