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Molecular interactions of the CcdB poison with its bacterial target, the DNA gyrase.

par Van Melderen, Laurence
Référence International journal of medical microbiology, 291, 6-7, page (537-544)
Publication Publié, 2002-02

Article révisé par les pairs

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Résumé :

The ccd poison/antidote system of the F plasmid encodes CcdB, a toxin targeting the essential DNA gyrase of E. coli, and CcdA, the unstable antidote that interacts with CcdB to neutralise its toxicity. Gyrase belongs to the topoisomerase II class of enzymes and is a well-validated target for efficient therapeutic drugs, i. e. the quinolones. CcdB acts on gyrase in a similar way as quinolones do, both compounds induce double-strand breaks in DNA. Interestingly, the CcdB-binding domain of gyrase is different than that of quinolones. Therefore, novel classes of therapeutic drugs could be derived from the analysis of the interaction between CcdB and gyrase.