6F8H
antitoxin GraA
Summary for 6F8H
| Entry DOI | 10.2210/pdb6f8h/pdb |
| Descriptor | XRE family transcriptional regulator (2 entities in total) |
| Functional Keywords | graa, higa, antitoxin |
| Biological source | Pseudomonas putida (Arthrobacter siderocapsulatus) |
| Total number of polymer chains | 4 |
| Total formula weight | 46985.60 |
| Authors | Talavera, A.,Loris, R. (deposition date: 2017-12-13, release date: 2019-01-30, Last modification date: 2024-05-08) |
| Primary citation | Talavera, A.,Tamman, H.,Ainelo, A.,Konijnenberg, A.,Hadzi, S.,Sobott, F.,Garcia-Pino, A.,Horak, R.,Loris, R. A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. Nat Commun, 10:972-972, 2019 Cited by PubMed Abstract: Bacterial toxin-antitoxin (TA) modules are tightly regulated to maintain growth in favorable conditions or growth arrest during stress. A typical regulatory strategy involves the antitoxin binding and repressing its own promoter while the toxin often acts as a co-repressor. Here we show that Pseudomonas putida graTA-encoded antitoxin GraA and toxin GraT differ from other TA proteins in the sense that not the antitoxin but the toxin possesses a flexible region. GraA auto-represses the graTA promoter: two GraA dimers bind cooperatively at opposite sides of the operator sequence. Contrary to other TA modules, GraT is a de-repressor of the graTA promoter as its N-terminal disordered segment prevents the binding of the GraTA complex to the operator. Removal of this region restores operator binding and abrogates Gr aT toxicity. GraTA represents a TA module where a flexible region in the toxin rather than in the antitoxin controls operon expression and toxin activity. PubMed: 30814507DOI: 10.1038/s41467-019-08865-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.002 Å) |
Structure validation
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