8R64
Cryo-EM structure of the FIGNL1 AAA hexamer bound to RAD51
Summary for 8R64
| Entry DOI | 10.2210/pdb8r64/pdb |
| EMDB information | 18946 |
| Descriptor | Fidgetin-like protein 1, DNA repair protein RAD51 homolog 1, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | aaa, atpase, dna repair, hydrolase |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 7 |
| Total formula weight | 317045.09 |
| Authors | Carver, A.,Yates, L.A.,Zhang, X. (deposition date: 2023-11-20, release date: 2024-09-04, Last modification date: 2025-02-05) |
| Primary citation | Carver, A.,Yu, T.Y.,Yates, L.A.,White, T.,Wang, R.,Lister, K.,Jasin, M.,Zhang, X. Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin. Science, 387:426-431, 2025 Cited by PubMed Abstract: Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central player of several crucial processes in repairing DNA and protecting genome integrity, forms filaments on DNA, which are tightly regulated. One of these RAD51 regulators is FIGNL1, that prevents persistent RAD51 foci without or after DNA damage and genotoxic chromatin association in cells. The cryogenic electron microscopy structure of FIGNL1 in complex with RAD51 reveals that FIGNL1 forms a non-planar hexamer and RAD51 N terminus enclosure in the FIGNL1 hexamer pore. Mutations in pore loop or catalytic residues of FIGNL1 render it defective in filament disassembly and are lethal in mouse embryonic stem cells. Our study reveals a unique mechanism for removing RAD51 from bound substrates and provides the molecular basis for FIGNL1 in maintaining genome stability. PubMed: 39636933DOI: 10.1126/science.adr7920 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
Download full validation report
