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9svy

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XRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex) capping a RAD51 filament on partially duplex DNA

Structural highlights

9svy is a 13 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.6Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

RA51D_HUMAN Hereditary breast and/or ovarian cancer syndrome;Familial prostate cancer. Disease susceptibility is associated with variants affecting the gene represented in this entry.

Function

RA51D_HUMAN Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

References

↑ Braybrooke JP, Spink KG, Thacker J, Hickson ID. The RAD51 family member, RAD51L3, is a DNA-stimulated ATPase that forms a complex with XRCC2. J Biol Chem. 2000 Sep 15;275(37):29100-6. PMID:10871607 doi:10.1074/jbc.M002075200
↑ Masson JY, Tarsounas MC, Stasiak AZ, Stasiak A, Shah R, McIlwraith MJ, Benson FE, West SC. Identification and purification of two distinct complexes containing the five RAD51 paralogs. Genes Dev. 2001 Dec 15;15(24):3296-307. PMID:11751635 doi:10.1101/gad.947001
↑ Kurumizaka H, Ikawa S, Nakada M, Enomoto R, Kagawa W, Kinebuchi T, Yamazoe M, Yokoyama S, Shibata T. Homologous pairing and ring and filament structure formation activities of the human Xrcc2*Rad51D complex. J Biol Chem. 2002 Apr 19;277(16):14315-20. PMID:11834724 doi:10.1074/jbc.M105719200
↑ Liu N, Schild D, Thelen MP, Thompson LH. Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells. Nucleic Acids Res. 2002 Feb 15;30(4):1009-15. PMID:11842113 doi:10.1093/nar/30.4.1009
↑ Braybrooke JP, Li JL, Wu L, Caple F, Benson FE, Hickson ID. Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D). J Biol Chem. 2003 Nov 28;278(48):48357-66. PMID:12975363 doi:10.1074/jbc.M308838200
↑ Tarsounas M, Muñoz P, Claas A, Smiraldo PG, Pittman DL, Blasco MA, West SC. Telomere maintenance requires the RAD51D recombination/repair protein. Cell. 2004 Apr 30;117(3):337-47. PMID:15109494 doi:10.1016/s0092-8674(04)00337-x
↑ Chun J, Buechelmaier ES, Powell SN. Rad51 paralog complexes BCDX2 and CX3 act at different stages in the BRCA1-BRCA2-dependent homologous recombination pathway. Mol Cell Biol. 2013 Jan;33(2):387-95. PMID:23149936 doi:10.1128/MCB.00465-12