The interaction of DNA gyrase with the bacterial toxin CcdB: evidence for the existence of two gyrase-CcdB complexes.
作者： Sotirios C. Kampranis , Alison J. Howells , Anthony Maxwell
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摘要: CcdB is a bacterial toxin that targets DNA gyrase. Analysis of the interaction with gyrase reveals two distinct complexes. An initial complex (alpha) formed by direct between GyrA and CcdB; this can be detected affinity column gel-shift analysis, has proteolytic signature which characterised 49 kDa fragment GyrA. Surface plasmon resonance shows binds to N-terminal domain high affinity. In mode binding, does not affect ability hydrolyse ATP or promote supercoiling. Incubation in presence GyrB slowly converts it second (beta), lower rate hydrolysis unable catalyse The efficiency formation inactive dependent on concentrations CcdB. We suggest conversion complexes proceeds via an intermediate, whose hydrolysis.
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