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

被引:52
作者
Doré, AS
Furnham, N
Davies, OR
Sibanda, BL
Chirgadze, DY
Jackson, SP
Pellegrini, L
Blundell, TL
机构
[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England
[2] Univ Cambridge, Dept Zool, Cambridge CB2 1QR, England
[3] Univ Cambridge, Gurdon Inst, Wellcome Trust & Canc UK, Cambridge CB2 1QR, England
基金
英国惠康基金;
关键词
DNA repair; Xrcc4; DNA ligase IV; BRCT; coiled-coil;
D O I
10.1016/j.dnarep.2005.11.004
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
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 angstrom 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. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码:362 / 368
页数:7
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