1z56
Co-Crystal Structure of Lif1p-Lig4pCo-Crystal Structure of Lif1p-Lig4p
Structural highlights
Function[DNLI4_YEAST] Has minor DNA joining activity. Can act on oligo(PDT)/poly(rA) substrate. [LIF1_YEAST] Stabilizes DNL4. Involved in non-homologous repair of DNA double-strand breaks.[1] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDNA 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. Structure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode.,Dore AS, Furnham N, Davies OR, Sibanda BL, Chirgadze DY, Jackson SP, Pellegrini L, Blundell TL DNA Repair (Amst). 2006 Mar 7;5(3):362-8. Epub 2006 Jan 18. PMID:16388993[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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