Structure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode.
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.
Mesh Terms:
Amino Acid Sequence, BRCA1 Protein, Crystallization, Crystallography, X-Ray, DNA Damage, DNA Ligases, DNA Repair, DNA, Fungal, DNA-Binding Proteins, Molecular Sequence Data, Molecular Structure, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid
Amino Acid Sequence, BRCA1 Protein, Crystallization, Crystallography, X-Ray, DNA Damage, DNA Ligases, DNA Repair, DNA, Fungal, DNA-Binding Proteins, Molecular Sequence Data, Molecular Structure, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid
DNA Repair (Amst.)
Date: Mar. 07, 2006
PubMed ID: 16388993
View in: Pubmed Google Scholar
Download Curated Data For This Publication
68181
Switch View:
- Interactions 1