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- W1982757640 abstract "The diphtheria toxin repressor (DtxR) is a metal ion-activated transcriptional regulator that has been linked to the virulence of Corynebacterium diphtheriae . Structure determination has shown that there are two metal ion binding sites per repressor monomer, and site-directed mutagenesis has demonstrated that binding site 2 (primary) is essential for recognition of the target DNA repressor, leaving the role of binding site 1 (ancillary) unclear. Calorimetric techniques have demonstrated that although binding site 1 (ancillary) has high affinity for metal ion with a binding constant of 2 × 10 –7 , binding site 2 (primary) is a low-affinity binding site with a binding constant of 6.3 × 10 –4 . These two binding sites act in an independent fashion, and their contribution can be easily dissected by traditional mutational analysis. Our results clearly demonstrate that binding site 1 (ancillary) is the first one to be occupied during metal ion activation, playing a critical role in stabilization of the repressor. In addition, structural data obtained for the mutants Ni-DtxR(H79A,C102D), reported here, and the previously reported DtxR(H79A) have allowed us to propose a mechanism of metal activation for DtxR." @default.
- W1982757640 created "2016-06-24" @default.
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- W1982757640 date "2005-12-13" @default.
- W1982757640 modified "2023-10-03" @default.
- W1982757640 title "Mechanism of metal ion activation of the diphtheria toxin repressor DtxR" @default.
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- W1982757640 doi "https://doi.org/10.1073/pnas.0500908102" @default.
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