1Z56
Co-Crystal Structure of Lif1p-Lig4p
Summary for 1Z56
Entry DOI | 10.2210/pdb1z56/pdb |
Descriptor | Ligase interacting factor 1, DNA ligase IV, ... (9 entities in total) |
Functional Keywords | dna repair, brct, nhej, xrcc4, dna ligase, coiled-coil, ligase |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Cellular location | Cytoplasm : P53150 Nucleus : Q08387 |
Total number of polymer chains | 11 |
Total formula weight | 102072.38 |
Authors | Dore, A.S.,Furnham, N.,Davies, O.R.,Sibanda, B.L.,Chirgadze, D.Y.,Jackson, S.P.,Pellegrini, L.,Blundell, T.L. (deposition date: 2005-03-17, release date: 2006-01-31, Last modification date: 2024-02-14) |
Primary citation | Dore, A.S.,Furnham, N.,Davies, O.R.,Sibanda, B.L.,Chirgadze, D.Y.,Jackson, S.P.,Pellegrini, L.,Blundell, T.L. Structure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode. DNA REPAIR, 5:362-368, 2006 Cited by PubMed 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. PubMed: 16388993DOI: 10.1016/j.dnarep.2005.11.004 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.92 Å) |
Structure validation
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