Ring structure of the Escherichia coli DNA-binding protein RdgC associated with recombination and replication fork repair.

@article{Briggs2007RingSO,
  title={Ring structure of the Escherichia coli DNA-binding protein RdgC associated with recombination and replication fork repair.},
  author={Geoffrey S Briggs and Paul A. McEwan and Jing Yu and Timothy Michael Moore and Jonas Emsley and R. G. Lloyd},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 17},
  pages={12353-7}
}
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… CONTINUE READING