Ring structure of the Escherichia coli DNA-binding protein RdgC associated with recombination and replication fork repair.
J Biol Chem
; 282(17): 12353-7, 2007 Apr 27.
Article
em En
| MEDLINE
| ID: mdl-17308310
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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Bases de dados:
MEDLINE
Assunto principal:
Proteínas de Escherichia coli
/
Proteínas de Ligação a DNA
/
Escherichia coli
Tipo de estudo:
Risk_factors_studies
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
2007
Tipo de documento:
Article