Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine.

@article{Jo2016CrystalSO,
  title={Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine.},
  author={Chang Hwa Jo and Junsoo Kim and Ah-Reum Han and Sam Park and Kwang Yeon Hwang and Ki Hyun Nam},
  journal={FEBS letters},
  year={2016},
  volume={590 6},
  pages={848-56}
}
Site-specific Xer recombination plays a pivotal role in reshuffling genetic information. Here, we report the 2.5 Å crystal structure of XerA from the archaean Thermoplasma acidophilum. Crystallographic data reveal a uniquely open conformational state, resulting in a C-shaped clamp with an angle of ~ 48° and a distance of 57 Å between the core-binding and the catalytic domains. The catalytic nucleophile, Tyr264, is positioned in cis-cleavage mode by XerA's C-term tail that interacts with the CAT… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 2 times over the past 90 days. VIEW TWEETS

References

Publications referenced by this paper.
Showing 1-10 of 34 references

The carboxy-terminal alphaN helix of the archaeal XerA tyrosine recombinase is a molecular switch to control site

  • MC Serre, T El Arnaout, +6 authors S Quevillon-Cheruel
  • 2013

Similar Papers

Loading similar papers…