2OWL

Ring Structure of the Escherichia coli DNA-binding Protein RdgC Associated with Recombination and Replication Fork Repair.

(2007) J Biol Chem 282: 12353-12357

• PubMed: 17308310 Search on PubMed
• DOI: https://doi.org/10.1074/jbc.C700023200
• Primary Citation of Related Structures:  
  2OWL


• PubMed Abstract: 
  

  The DNA-binding protein, RdgC, is associated with recombination and replication fork repair in Escherichia coli and with the virulence-associated, pilin antigenic variation mediated by RecA and other recombination proteins in Neisseria species. We solved the structure of the E. coli protein and refined it to 2.4A. RdgC crystallizes as a dimer with a head-to-head, tail-to-tail organization forming a ring with a 30 A diameter hole at the center. The protein fold is unique and reminiscent of a horseshoe with twin gates closing the open end. The central hole is lined with positively charged residues and provides a highly plausible DNA binding channel consistent with the nonspecific mode of binding detected in vitro and with the ability of RdgC to modulate RecA function in vivo.

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Organizational Affiliation: 

Institute of Genetics, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH.