Nucleotide binding to the 43-kilodalton N-terminal fragment of the DNA gyrase B protein.

@article{Ali1995NucleotideBT,
  title={Nucleotide binding to the 43-kilodalton N-terminal fragment of the DNA gyrase B protein.},
  author={Janid A Ali and George Orphanides and Anthony Maxwell},
  journal={Biochemistry},
  year={1995},
  volume={34 30},
  pages={
          9801-8
        }
}
The binding of ADPNP (5'-adenylyl beta,gamma-imidodiphosphate) to the 43-kDa N-terminal fragment of the DNA gyrase B protein is found to stabilize a dimer of the protein. Analysis of the kinetics of binding of ADPNP to the fragment suggests that protein dimers can contain 1 or 2 molecules of bound nucleotide. ATP, ADP, or coumarin drugs inhibit the binding of ADPNP. The rate of dissociation of ADPNP from the 43-kDa protein is found to be very slow and unaffected by the presence of other… CONTINUE READING
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