4FCX
S.pombe Mre11 apoenzym
4FCX の概要
エントリーDOI | 10.2210/pdb4fcx/pdb |
関連するPDBエントリー | 4fbk 4fbq 4fbw |
分子名称 | DNA repair protein rad32, MANGANESE (II) ION (2 entities in total) |
機能のキーワード | dna double-strand break repair, nuclease, hydrolase |
由来する生物種 | Schizosaccharomyces pombe (Fission yeast) |
細胞内の位置 | Nucleus : Q09683 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 91542.74 |
構造登録者 | |
主引用文献 | Schiller, C.B.,Lammens, K.,Guerini, I.,Coordes, B.,Feldmann, H.,Schlauderer, F.,Mockel, C.,Schele, A.,Strasser, K.,Jackson, S.P.,Hopfner, K.P. Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. Nat.Struct.Mol.Biol., 19:693-700, 2012 Cited by PubMed Abstract: The Mre11-Rad50-Nbs1 (MRN) complex tethers, processes and signals DNA double-strand breaks, promoting genomic stability. To understand the functional architecture of MRN, we determined the crystal structures of the Schizosaccharomyces pombe Mre11 dimeric catalytic domain alone and in complex with a fragment of Nbs1. Two Nbs1 subunits stretch around the outside of the nuclease domains of Mre11, with one subunit additionally bridging and locking the Mre11 dimer via a highly conserved asymmetrical binding motif. Our results show that Mre11 forms a flexible dimer and suggest that Nbs1 not only is a checkpoint adaptor but also functionally influences Mre11-Rad50. Clinical mutations in Mre11 are located along the Nbs1-interaction sites and weaken the Mre11-Nbs1 interaction. However, they differentially affect DNA repair and telomere maintenance in Saccharomyces cerevisiae, potentially providing insight into their different human disease pathologies. PubMed: 22705791DOI: 10.1038/nsmb.2323 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3 Å) |
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