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PDBsum entry 3fyh

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protein ligands metals links
Recombination PDB id
3fyh

 

 

 

 

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Contents
Protein chain
296 a.a. *
Ligands
ADP
Metals
__W ×24
_MG ×2
_NA
Waters ×123
* Residue conservation analysis
PDB id:
3fyh
Name: Recombination
Title: Recombinase in complex with adp and metatungstate
Structure: DNA repair and recombination protein rada. Chain: a. Engineered: yes. Mutation: yes
Source: Methanococcus voltae. Organism_taxid: 2188. Gene: rada. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.200     R-free:   0.227
Authors: Y.Li,Y.He,Y.Luo
Key ref: 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
Date:
22-Jan-09     Release date:   01-Sep-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O73948  (RADA_METVO) -  DNA repair and recombination protein RadA from Methanococcus voltae
Seq:
Struc:
322 a.a.
296 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Biochemistry 48:6805-6810 (2009)
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.
 

 

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