Ring structure of the Escherichia coli DNA-binding protein RdgC associated with recombination and replication fork repair.
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.
Briggs
Geoffrey S
GS
Institute of Genetics, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH.
McEwan
Paul A
PA
Yu
Jing
J
Moore
Timothy
T
Emsley
Jonas
J
Lloyd
Robert G
RG
D004260:DNA Repair; D004261:DNA Replication; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D019281:Dimerization; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D036781:Fimbriae Proteins / Q000378:metabolism; D008958:Models, Molecular; D009343:Neisseria / Q000378:metabolism / Q000472:pathogenicity; D020836:Protein Structure, Quaternary; D011938:Rec A Recombinases / Q000378:metabolism; D011995:Recombination, Genetic
D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C103478:RdgC protein, E coli; D036781:Fimbriae Proteins; D011938:Rec A Recombinases