7YZO
Endonuclease state of the E. coli Mre11-Rad50 (SbcCD) head complex bound to ADP and dsDNA
Summary for 7YZO
| Entry DOI | 10.2210/pdb7yzo/pdb |
| EMDB information | 14391 |
| Descriptor | Nuclease SbcCD subunit C, Nuclease SbcCD subunit D, DNA (31-MER), ... (7 entities in total) |
| Functional Keywords | abc-type atpase, nuclease, dna repair, dna binding protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 6 |
| Total formula weight | 404176.48 |
| Authors | Gut, F.,Kaeshammer, L.,Lammens, K.,Bartho, J.,van de Logt, E.,Kessler, B.,Hopfner, K.P. (deposition date: 2022-02-21, release date: 2022-08-17, Last modification date: 2024-07-17) |
| Primary citation | Gut, F.,Kashammer, L.,Lammens, K.,Bartho, J.D.,Boggusch, A.M.,van de Logt, E.,Kessler, B.,Hopfner, K.P. Structural mechanism of endonucleolytic processing of blocked DNA ends and hairpins by Mre11-Rad50. Mol.Cell, 82:3513-3522.e6, 2022 Cited by PubMed Abstract: DNA double-strand breaks (DSBs) threaten genome stability and are linked to tumorigenesis in humans. Repair of DSBs requires the removal of attached proteins and hairpins through a poorly understood but physiologically critical endonuclease activity by the Mre11-Rad50 complex. Here, we report cryoelectron microscopy (cryo-EM) structures of the bacterial Mre11-Rad50 homolog SbcCD bound to a protein-blocked DNA end and a DNA hairpin. The structures reveal that Mre11-Rad50 bends internal DNA for endonucleolytic cleavage and show how internal DNA, DNA ends, and hairpins are processed through a similar ATP-regulated conformational state. Furthermore, Mre11-Rad50 is loaded onto blocked DNA ends with Mre11 pointing away from the block, explaining the distinct biochemistries of 3' → 5' exonucleolytic and endonucleolytic incision through the way Mre11-Rad50 interacts with diverse DNA ends. In summary, our results unify Mre11-Rad50's enigmatic nuclease diversity within a single structural framework and reveal how blocked DNA ends and hairpins are processed. PubMed: 35987200DOI: 10.1016/j.molcel.2022.07.019 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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