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-Structure paper
| タイトル | Structure guided functional analysis of the S. cerevisiae Mre11 complex. |
|---|---|
| ジャーナル・号・ページ | Nat Commun, Vol. 16, Issue 1, Page 7469, Year 2025 |
| 掲載日 | 2025年8月12日 |
著者 | Marcel Hohl / You Yu / Vitaly Kuryavyi / Dinshaw J Patel / John Petrini / ![]() |
| PubMed 要旨 | The Mre11 complex comprises Mre11, Rad50 and Nbs1 (Xrs2 in S. cerevisiae). The core components, Mre11 and Rad50 are highly conserved, with readily identifiable orthologs in all clades of life, ...The Mre11 complex comprises Mre11, Rad50 and Nbs1 (Xrs2 in S. cerevisiae). The core components, Mre11 and Rad50 are highly conserved, with readily identifiable orthologs in all clades of life, whereas Nbs1/Xrs2 are present only in eukaryotes. In eukaryotes, the complex is integral to the DNA damage response, acting in DNA double strand break (DSB) detection and repair, and the activation of DNA damage signaling. We present here a 3.2 Å cryo-EM structure of the S. cerevisiae Mre11-Rad50 complex with bound dsDNA. The structure provided a foundation for detailed mutational analyses regarding homo and heterotypic protein interfaces, as well as DNA binding properties of Rad50. We define several conserved residues in Rad50 and Mre11 that are critical to complex assembly as well as for DNA binding. In addition, the data reveal that the Rad50 coiled coil domain influences ATP hydrolysis over long distances. |
リンク | Nat Commun / PubMed:40796731 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.5 Å |
| 構造データ | EMDB-44559, PDB-9bi5: |
| 化合物 | ![]() ChemComp-ATP: ![]() ChemComp-MN: |
| 由来 |
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キーワード | DNA BINDING PROTEIN / MRN / Mre11 / Rad50 / Nbs1 / DNA binding / DNA damage / DNA repair |
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