Nature Communications (Jan 2022)

Topoisomerase I (TOP1) dynamics: conformational transition from open to closed states

  • Diane T. Takahashi,
  • Danièle Gadelle,
  • Keli Agama,
  • Evgeny Kiselev,
  • Hongliang Zhang,
  • Emilie Yab,
  • Stephanie Petrella,
  • Patrick Forterre,
  • Yves Pommier,
  • Claudine Mayer

DOI
https://doi.org/10.1038/s41467-021-27686-7
Journal volume & issue
Vol. 13, no. 1
pp. 1 – 11

Abstract

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Topoisomerase I (TOP1) relaxes both positive and negative supercoils by nicking DNA and after rotation of the broken DNA strand closes the nick. Here, the authors present the DNA free crystal structure of TOP1 from the hyperthermophilic archaeon Caldiarchaeum subterraneum in the open form and discuss the mechanism of how DNA enters the catalytic site of TOP1.