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 refi...

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Bibliographic Details
Published in:The Journal of biological chemistry 2007-04, Vol.282 (17), p.12353-12357
Main Authors: Briggs, Geoffrey S., McEwan, Paul A., Yu, Jing, Moore, Timothy, Emsley, Jonas, Lloyd, Robert G.
Format: Article
Language:English
Subjects:
Dimerization
DNA Repair
DNA Replication
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
Escherichia coli
Escherichia coli - chemistry
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Fimbriae Proteins - metabolism
Models, Molecular
Neisseria
Neisseria - metabolism
Neisseria - pathogenicity
Protein Structure, Quaternary
Rec A Recombinases - metabolism
Recombination, Genetic
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Summary: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 2.4Å. RdgC crystallizes as a dimer with a head-to-head, tail-to-tail organization forming a ring with a 30Å 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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.C700023200