Structural highlights
Function
RADA_METVO Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Archaeal RadAs are close homologues of eukaryal Rad51s ( approximately 40% sequence identities). These recombinases promote a hallmark strand exchange process between homologous single-stranded and double-stranded DNA substrates. This DNA-repairing function also plays a key role in cancer cells' resistance to chemo- and radiotherapy. Inhibition of the strand exchange process may render cancer cells more susceptible to therapeutic treatment. We found that metatungstate is a potent inhibitor of RadA from Methanococcus voltae. The tungsten cluster binds RadA in the axial DNA-binding groove. This polyanionic species appears to inhibit RadA by locking the protein in its inactive conformation.
Crystal structure of an archaeal Rad51 homologue in complex with a metatungstate inhibitor.,Li Y, He Y, Luo Y Biochemistry. 2009 Jul 28;48(29):6805-10. PMID:19555119[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li Y, He Y, Luo Y. Crystal structure of an archaeal Rad51 homologue in complex with a metatungstate inhibitor. Biochemistry. 2009 Jul 28;48(29):6805-10. PMID:19555119 doi:10.1021/bi900832t
