Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation
oleh: Morgan Jones, Fabienne Beuron, Aaron Borg, Andrea Nans, Christopher P. Earl, David C. Briggs, Ambrosius P. Snijders, Maureen Bowles, Edward P. Morris, Mark Linch, Neil Q. McDonald
| Format: | Article |
|---|---|
| Diterbitkan: | Nature Portfolio 2020-02-01 |
Deskripsi
The endonuclease XPF-ERCC1 is a key component of the repair machinery to process both intra-strand and inter-strand DNA crosslinks. Here the authors present the cryo-EM structures of DNA-free and DNA-bound human XPF-ERCC1 and find that DNA-free XPF-ERCC1 adopts an auto-inhibited conformation, which is opened up upon DNA binding and they also characterise the biochemical properties of patient-derived XPF-ERCC1 mutations.