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3FYH

Recombinase in complex with ADP and metatungstate

Summary for 3FYH
Entry DOI10.2210/pdb3fyh/pdb
Related2F1J
DescriptorDNA repair and recombination protein radA, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordsatpase, rada, rad51, reca, recombinase, inhibitor, rada-inhibitor complex, atp-binding, dna damage, dna recombination, dna-binding, nucleotide-binding, recombination
Biological sourceMethanococcus voltae
Total number of polymer chains1
Total formula weight40109.89
Authors
Li, Y.,He, Y.,Luo, Y. (deposition date: 2009-01-22, release date: 2009-09-01, Last modification date: 2023-09-06)
Primary citationLi, 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: 19555119
DOI: 10.1021/bi900832t
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

237992

数据于2025-06-25公开中

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