ATP binding controls distinct structural transitions of Escherichia coli DNA gyrase in complex with DNA

@inproceedings{Basu2012ATPBC,
  title={ATP binding controls distinct structural transitions of Escherichia coli DNA gyrase in complex with DNA},
  author={Aakash Basu and Allyn J. Schoeffler and James M Berger and Zev Bryant},
  booktitle={Nature Structural &Molecular Biology},
  year={2012}
}
DNA gyrase is a molecular motor that harnesses the free energy of ATP hydrolysis to introduce negative supercoils into DNA. A critical step in this reaction is the formation of a chiral DNA wrap. Here we observe gyrase structural dynamics using a single-molecule assay in which gyrase drives the processive, stepwise rotation of a nanosphere attached to the side of a stretched DNA molecule. Analysis of rotational pauses and measurements of DNA contraction reveal multiple ATP-modulated structural… CONTINUE READING

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