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PDBsum entry 6f8s

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Toxin PDB id
6f8s
Contents
Protein chains
94 a.a.
66 a.a.
65 a.a.
Ligands
SO4 ×2
PEG ×3
Waters ×11

References listed in PDB file
Key reference
Title A dual role in regulation and toxicity for the disordered n-Terminus of the toxin grat.
Authors A.Talavera, H.Tamman, A.Ainelo, A.Konijnenberg, S.HadžI, F.Sobott, A.Garcia-Pino, R.Hõrak, R.Loris.
Ref. Nat Commun, 2019, 10, 972. [DOI no: 10.1038/s41467-019-08865-z]
PubMed id 30814507
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 GraT2A2 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.
Secondary reference #1
Title Production, Biophysical characterization and crystallization of pseudomonas putida graa and its complexes with grat and the grata operator.
Authors A.Talavera, H.Tamman, A.Ainelo, S.HadǽI, A.Garcia-Pino, R.Hõrak, A.Konijnenberg, R.Loris.
Ref. Acta Crystallogr F Struct Biol Commun, 2017, 73, 455-462. [DOI no: 10.1107/S2053230X17009438]
PubMed id 28777088
Abstract
PROCHECK
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