Summary information and primary citation
- PDB-id
-
9sw0;
DSSR-derived features in text and
JSON formats
- Class
- DNA binding protein
- Method
- cryo-EM (3.0 Å)
- Summary
- Xrcc3-rad51c-rad51d-xrcc2 (xrcc3 complex) capping a
rad51 filament on a d-loop intermediate
- Reference
-
Greenhough LA, Galanti L, Liang CC, Boulton SJ, West SC
(2025): "Cryo-electron
microscopy visualization of RAD51 filament assembly and
end-capping by XRCC3-RAD51C-RAD51D-XRCC2."
Science, eaea1546. doi: 10.1126/science.aea1546.
- Abstract
- Homologous recombination repairs DNA double strand
breaks and protects stalled replication forks, but how the
five RAD51 paralogs contribute to these processes remains
unclear. Mutations in the RAD51 paralogs are linked to
heritable breast and ovarian cancers and the cancer-prone
disease Fanconi anemia. In this work, we show that the
RAD51 paralogs assemble into two distinct heterotetrameric
complexes, RAD51B-RAD51C-RAD51D-XRCC2 (RAD51B complex) and
XRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex). The RAD51B
complex promotes dynamic adenosine triphosphate
hydrolysis-dependent assembly of RAD51 filaments, whereas
the XRCC3 complex stably caps the 5'-termini of RAD51
filaments to promote homologous pairing, as visualized by
cryo-electron microscopy. Highly conserved across
evolution, these complexes reveal insights into RAD51
filament formation and capping during DNA repair and
replication fork stabilization.
