1L8D

Rad50 coiled-coil Zn hook

1L8D の概要

• エントリーDOI: 10.2210/pdb1l8d/pdb
• 関連するPDBエントリー: 1F2T 1F2U 1II7 1II8
• 分子名称: DNA double-strand break repair rad50 ATPase, MERCURY (II) ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: zinc finger, rad50, dna repair, recombination, hook motif, replication
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27269.14

構造登録者

Hopfner, K.P.,Tainer, J.A. (登録日: 2002-03-20, 公開日: 2002-08-28, 最終更新日: 2024-05-22)

主引用文献

Hopfner, K.P.,Craig, L.,Moncalian, G.,Zinkel, R.A.,Usui, T.,Owen, B.A.,Karcher, A.,Henderson, B.,Bodmer, J.L.,McMurray, C.T.,Carney, J.P.,Petrini, J.H.,Tainer, J.A.
The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair.
Nature, 418:562-566, 2002

PubMed Abstract: The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal maintenance and functions in homologous recombination, telomere maintenance and sister chromatid association. These functions all imply that the linked binding of two DNA substrates occurs, although the molecular basis for this process remains unknown. Here we present a 2.2 A crystal structure of the Rad50 coiled-coil region that reveals an unexpected dimer interface at the apex of the coiled coils in which pairs of conserved Cys-X-X-Cys motifs form interlocking hooks that bind one Zn(2+) ion. Biochemical, X-ray and electron microscopy data indicate that these hooks can join oppositely protruding Rad50 coiled-coil domains to form a flexible bridge of up to 1,200 A. This suggests a function for the long insertion in the Rad50 ABC-ATPase domain. The Rad50 hook is functional, because mutations in this motif confer radiation sensitivity in yeast and disrupt binding at the distant Mre11 nuclease interface. These data support an architectural role for the Rad50 coiled coils in forming metal-mediated bridging complexes between two DNA-binding heads. The resulting assemblies have appropriate lengths and conformational properties to link sister chromatids in homologous recombination and DNA ends in non-homologous end-joining.

PubMed: 12152085
DOI: 10.1038/nature00922

実験手法

X-RAY DIFFRACTION (2.2 Å)