Main > PNEUMOLOGY > Tuberculosis > Drug Resistance > AntiBiotics Drug Resistance > Org.: USA. A (DNA-Mimic Protein) > MfpA>Structure/Mechanism

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The team s 2.0-Å-resolution picture of MfpA shows that the dimeric protein folds into a right-handed helix, with extensive hydrogen-bonding interactions between the peptide backbone atoms of adjacent square-shaped coils. The protein s overall size, shape, and charge distribution closely mimic that of normal B-form DNA.

The similarity to DNA has led team to suggest that MfpA and its relatives interact directly with DNA gyrase. They demonstrate that MfpA fits nicely into the enzyme s DNA-binding site. Blanchard suggests that, in the presence of MfpA, DNA gyrase does not form the DNA-bound gyrase complex that is the fluoroquinolone target, rendering the drug useless.

This novel mechanism may be responsible for the rapid spread of fluoroquinolone resistance that is making multi-drug-resistant bacterial infections so difficult to treat, author says. The new structure also suggests that the sequence of MfpA could be tweaked to design DNA mimics that specifically target other DNA-binding proteins.



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