Structure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode.
- Abstract:
- DNA ligase IV catalyses the final ligation step in the non-homologous end-joining (NHEJ) DNA repair pathway and requires interaction of the ligase with the Xrcc4 'genome-guardian', an essential NHEJ factor. Here we report the 3.9 A crystal structure of the Saccharomyces cerevisiae Xrcc4 ortholog ligase interacting factor 1 (Lif1p) complexed with the C-terminal BRCT domains of DNA ligase IV (Lig4p). The structure reveals a novel mode of protein recognition by a tandem BRCT repeat, and in addition provides a molecular basis for a human LIG4 syndrome clinical condition.
- Authors:
- AS Doré, N Furnham, OR Davies, BL Sibanda, DY Chirgadze, SP Jackson, L Pellegrini, TL Blundell
- Journal:
- DNA Repair (Amst)
- Citation info:
- 5(3):362-368
- Publication date:
- 7th Mar 2006
- Full text
- DOI