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TitleCryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 1120, Year 2020
Publish dateFeb 28, 2020
AuthorsMorgan 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 /
PubMed AbstractThe structure-specific endonuclease XPF-ERCC1 participates in multiple DNA damage repair pathways including nucleotide excision repair (NER) and inter-strand crosslink repair (ICLR). How XPF-ERCC1 is ...The structure-specific endonuclease XPF-ERCC1 participates in multiple DNA damage repair pathways including nucleotide excision repair (NER) and inter-strand crosslink repair (ICLR). How XPF-ERCC1 is catalytically activated by DNA junction substrates is not currently understood. Here we report cryo-electron microscopy structures of both DNA-free and DNA-bound human XPF-ERCC1. DNA-free XPF-ERCC1 adopts an auto-inhibited conformation in which the XPF helical domain masks the ERCC1 (HhH) domain and restricts access to the XPF catalytic site. DNA junction engagement releases the ERCC1 (HhH) domain to couple with the XPF-ERCC1 nuclease/nuclease-like domains. Structure-function data indicate xeroderma pigmentosum patient mutations frequently compromise the structural integrity of XPF-ERCC1. Fanconi anaemia patient mutations in XPF often display substantial in-vitro activity but are resistant to activation by ICLR recruitment factor SLX4. Our data provide insights into XPF-ERCC1 architecture and catalytic activation.
External linksNat Commun / PubMed:32111838 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 7.9 Å
Structure data

10337

6sxa

EMDB-10337, PDB-6sxa:
XPF-ERCC1 Cryo-EM Structure, Apo-form
Method: EM (single particle) / Resolution: 3.6 Å

10338

6sxb

EMDB-10338, PDB-6sxb:
XPF-ERCC1 Cryo-EM Structure, DNA-Bound form
Method: EM (single particle) / Resolution: 7.9 Å

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN / DNA Repair enzyme. Nucleotide excision repair

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