3FYH
Recombinase in complex with ADP and metatungstate
Summary for 3FYH
Entry DOI | 10.2210/pdb3fyh/pdb |
Related | 2F1J |
Descriptor | DNA repair and recombination protein radA, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total) |
Functional Keywords | atpase, rada, rad51, reca, recombinase, inhibitor, rada-inhibitor complex, atp-binding, dna damage, dna recombination, dna-binding, nucleotide-binding, recombination |
Biological source | Methanococcus voltae |
Total number of polymer chains | 1 |
Total formula weight | 40109.89 |
Authors | |
Primary citation | Li, Y.,He, Y.,Luo, Y. Crystal structure of an archaeal Rad51 homologue in complex with a metatungstate inhibitor. Biochemistry, 48:6805-6810, 2009 Cited by PubMed 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. PubMed: 19555119DOI: 10.1021/bi900832t PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
