9NJK
The Cryo-EM structure of the yeast Rad51-ssDNA nucleoprotein filament ADP bound state
Summary for 9NJK
| Entry DOI | 10.2210/pdb9njk/pdb |
| EMDB information | 49485 |
| Descriptor | DNA repair protein RAD51, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | dna repair, homologous recombination, dna binding protein |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) |
| Total number of polymer chains | 6 |
| Total formula weight | 259849.99 |
| Authors | Shin, Y.,Greene, E.C. (deposition date: 2025-02-27, release date: 2025-03-19, Last modification date: 2025-10-01) |
| Primary citation | Shin, Y.,Kim, S.Y.,Greene, E.C. ATP hydrolysis-driven structural transitions within the Saccharomyces cerevisiae Rad51 and Dmc1 nucleoprotein filaments. J.Biol.Chem., 301:110528-110528, 2025 Cited by PubMed Abstract: Homologous recombination (HR) is essential for the maintenance of genome stability and for generating genetic diversity during meiosis. The eukaryotic protein Rad51 is member of the Rad51/RecA family of DNA recombinases and is responsible for guiding the DNA pairing reactions that take place in HR during mitosis. Dmc1 is a meiosis-specific paralog of Rad51 and is responsible for the DNA pairing reactions that take place in HR during meiosis. Rad51 and Dmc1 are both ATP-dependent DNA-binding proteins and both form extended helical filaments on ssDNA, which are key intermediates in HR. The stability of these nucleoprotein filaments is highly regulated and is also tightly coupled to nucleotide binding and hydrolysis. ATP binding promotes filament assembly, whereas the hydrolysis of ATP to ADP reduces filament stability to promote filament disassembly. Here, we present cryo-EM structures of the Saccharomyces cerevisiae recombinases Rad51 and Dmc1 in the ADP-bound states and provide a detailed structural comparison to the ATP-bound filaments. Our findings yield insights into the structural transitions that take place during the hydrolysis of ATP to ADP and suggest a new model for how these structural changes may be linked to nucleoprotein filament disassembly. PubMed: 40721016DOI: 10.1016/j.jbc.2025.110528 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.37 Å) |
Structure validation
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