Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I

@article{Lima1994ThreedimensionalSO,
  title={Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I},
  author={Christopher D. Lima and James C. Wang and Alfonso Mondrag{\'o}n},
  journal={Nature},
  year={1994},
  volume={367},
  pages={138-146}
}
The three-dimensional structure of the 67K amino-terminal fragment of Escherichia coli DNA topoisomerase I has been determined to 2.2 Å resolution. The polypeptide folds in an unusual way to give four distinct domains enclosing a hole large enough to accommodate a double-stranded DNA. The active-site tyrosyl residue, which is involved in the transient breakage of a DNA strand and the formation of a covalent enzyme–DNA intermediate, is present at the interface of two domains. The structure… 

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...

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Escherichia coli omega protein, a type 1 topoisomerase, can catenate and knot duplex DNA circles. Previously, these activities were thought to be limited to type 2 topoisomerases. Catenation by omega

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