7ZR1
Chaetomium thermophilum Mre11-Rad50-Nbs1 complex bound to ATPyS (composite structure)
Summary for 7ZR1
| Entry DOI | 10.2210/pdb7zr1/pdb |
| Related | 7ZQY |
| EMDB information | 14876 14877 14878 14879 14880 14881 14882 |
| Descriptor | Double-strand break repair protein, DH domain-containing protein, FHA domain-containing protein, ... (6 entities in total) |
| Functional Keywords | dna repair, complex, atpase, coiled-coils, hydrolase |
| Biological source | Thermochaetoides thermophila More |
| Total number of polymer chains | 5 |
| Total formula weight | 577828.03 |
| Authors | Bartho, J.D.,Rotheneder, M.,Stakyte, K.,Lammens, K.,Hopfner, K.P. (deposition date: 2022-05-03, release date: 2023-01-11, Last modification date: 2023-12-13) |
| Primary citation | Rotheneder, M.,Stakyte, K.,van de Logt, E.,Bartho, J.D.,Lammens, K.,Fan, Y.,Alt, A.,Kessler, B.,Jung, C.,Roos, W.P.,Steigenberger, B.,Hopfner, K.P. Cryo-EM structure of the Mre11-Rad50-Nbs1 complex reveals the molecular mechanism of scaffolding functions. Mol.Cell, 83:167-185.e9, 2023 Cited by PubMed Abstract: The DNA double-strand break repair complex Mre11-Rad50-Nbs1 (MRN) detects and nucleolytically processes DNA ends, activates the ATM kinase, and tethers DNA at break sites. How MRN can act both as nuclease and scaffold protein is not well understood. The cryo-EM structure of MRN from Chaetomium thermophilum reveals a 2:2:1 complex with a single Nbs1 wrapping around the autoinhibited Mre11 nuclease dimer. MRN has two DNA-binding modes, one ATP-dependent mode for loading onto DNA ends and one ATP-independent mode through Mre11's C terminus, suggesting how it may interact with DSBs and intact DNA. MRNs two 60-nm-long coiled-coil domains form a linear rod structure, the apex of which is assembled by the two joined zinc-hook motifs. Apices from two MRN complexes can further dimerize, forming 120-nm spanning MRN-MRN structures. Our results illustrate the architecture of MRN and suggest how it mechanistically integrates catalytic and tethering functions. PubMed: 36577401DOI: 10.1016/j.molcel.2022.12.003 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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