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PDBsum entry 6f8h

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protein Protein-protein interface(s) links
Antitoxin PDB id
6f8h

 

 

 

 

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Contents
Protein chains
96 a.a.
Waters ×241
PDB id:
6f8h
Name: Antitoxin
Title: Antitoxin graa
Structure: Xre family transcriptional regulator. Chain: a, b, c, d. Engineered: yes
Source: Pseudomonas putida. Arthrobacter siderocapsulatus. Organism_taxid: 303. Gene: ayo08_18510. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693
Resolution:
2.00Å     R-factor:   0.192     R-free:   0.226
Authors: A.Talavera,R.Loris
Key ref: A.Talavera et al. (2019). A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. Nat Commun, 10, 972. PubMed id: 30814507 DOI: 10.1038/s41467-019-08865-z
Date:
13-Dec-17     Release date:   30-Jan-19    
PROCHECK
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 Headers
 References

Protein chains
A0A179R2V1  () - 
Key:    Secondary structure

 

 
DOI no: 10.1038/s41467-019-08865-z Nat Commun 10:972 (2019)
PubMed id: 30814507  
 
 
A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT.
A.Talavera, H.Tamman, A.Ainelo, A.Konijnenberg, S.Hadži, F.Sobott, A.Garcia-Pino, R.Hõrak, R.Loris.
 
  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.
 

 

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