Y.Li
et al.
(2009).
Crystal structure of an archaeal Rad51 homologue in complex with a metatungstate inhibitor.
Biochemistry,
48,
6805-6810.
PubMed id: 19555119
Crystal structure of an archaeal Rad51 homologue in complex with a metatungstate inhibitor.
Y.Li,
Y.He,
Y.Luo.
ABSTRACT
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.