Structure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode

Andrew S Doré, Nicholas Furnham, Owen R Davies, Bancinyane L Sibanda, Dimitri Y Chirgadze, Luca Pellegrini, Tom L Blundell

Research output: Contribution to journalArticlepeer-review

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 Å 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.
Original languageEnglish
Pages (from-to)362-368
Number of pages7
JournalDNA Repair
Volume5
Issue number3
Early online date18 Jan 2006
DOIs
Publication statusPublished - 7 Mar 2006

Keywords

  • DNA repair
  • Xrcc4
  • DNA ligase IV
  • BRCT
  • coiled-coils

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