Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad.

@article{Karakas2007StructureOT,
  title={Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad.},
  author={Erkan Karakas and James J Truglio and Deborah L. Croteau and Benjamin Rhau and Li-qun Wang and Bennett van Houten and Caroline Kisker},
  journal={The EMBO journal},
  year={2007},
  volume={26 2},
  pages={613-22}
}
Removal and repair of DNA damage by the nucleotide excision repair pathway requires two sequential incision reactions, which are achieved by the endonuclease UvrC in eubacteria. Here, we describe the crystal structure of the C-terminal half of UvrC, which contains the catalytic domain responsible for 5' incision and a helix-hairpin-helix-domain that is implicated in DNA binding. Surprisingly, the 5' catalytic domain shares structural homology with RNase H despite the lack of sequence homology… CONTINUE READING

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