7R5A
Vibrio cholera ParD2:ParE2 antitoxin:toxin complex
Summary for 7R5A
| Entry DOI | 10.2210/pdb7r5a/pdb |
| Descriptor | Toxin, Antitoxin ParD (2 entities in total) |
| Functional Keywords | prokaryotic toxin:antitoxin system, intrinsically disordered proteins, rhh protein, dna binding protein, transcriptional repressor, antitoxin, toxin, gyrase-poison, vibrio cholerae |
| Biological source | Vibrio cholerae O1 biovar El Tor str. N16961 More |
| Total number of polymer chains | 4 |
| Total formula weight | 39353.56 |
| Authors | Garcia-Rodriguez, G.,Loris, R. (deposition date: 2022-02-10, release date: 2022-04-27, Last modification date: 2024-01-31) |
| Primary citation | Garcia-Rodriguez, G.,Girardin, Y.,Kumar Singh, R.,Volkov, A.N.,Van Dyck, J.,Muruganandam, G.,Sobott, F.,Charlier, D.,Loris, R. Toxin:antitoxin ratio sensing autoregulation of the Vibrio cholerae parDE2 module. Sci Adv, 10:eadj2403-eadj2403, 2024 Cited by PubMed Abstract: The family of toxin-antitoxin (TA) operons is ubiquitous in bacterial genomes and, in , is an essential component to maintain the presence of chromosome II. Here, we show that transcription of the (Vc) operon is regulated in a toxin:antitoxin ratio-dependent manner using a molecular mechanism distinct from other type II TA systems. The repressor of the operon is identified as an assembly with a 6:2 stoichiometry with three interacting ParD2 dimers bridged by two ParE2 monomers. This assembly docks to a three-site operator containing 5'- GGTA-3' motifs. Saturation of this TA complex with ParE2 toxin results in disruption of the interface between ParD2 dimers and the formation of a TA complex of 2:2 stoichiometry. The latter is operator binding-incompetent as it is incompatible with the required spacing of the ParD2 dimers on the operator. PubMed: 38181072DOI: 10.1126/sciadv.adj2403 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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