Xrcc4-DNA连接酶IV酵母直系同源复合物的结构揭示了一种新的BRCT相互作用模式。
Structure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode.
作者信息
Doré Andrew S, Furnham Nicholas, Davies Owen R, Sibanda Bancinyane L, Chirgadze Dimitri Y, Jackson Stephen P, Pellegrini Luca, Blundell Tom L
机构信息
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB2 1GA, UK.
出版信息
DNA Repair (Amst). 2006 Mar 7;5(3):362-8. doi: 10.1016/j.dnarep.2005.11.004. Epub 2006 Jan 18.
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.
DNA连接酶IV催化非同源末端连接（NHEJ）DNA修复途径中的最终连接步骤，并且需要该连接酶与Xrcc4“基因组守护者”相互作用，Xrcc4是一种必不可少的NHEJ因子。在此，我们报道了酿酒酵母Xrcc4直系同源连接酶相互作用因子1（Lif1p）与DNA连接酶IV（Lig4p）的C末端BRCT结构域复合的3.9埃晶体结构。该结构揭示了串联BRCT重复序列识别蛋白质的新模式，此外还为人类LIG4综合征临床病症提供了分子基础。
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