RdgC protein employs a novel mechanism involving a finger domain to bind to circular DNA

The DNA-binding protein RdgC has been identified as an inhibitor of RecA-mediated homologous recombination in Escherichia coli. In Neisseria species, RdgC also has a role in virulence-associated antigenic variation. We have previously solved the crystal structure of the E. coli RdgC protein and show...

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Veröffentlicht in:	Nucleic acids research 2010-10, Vol.38 (19), p.6433-6446
Hauptverfasser:	Briggs, Geoffrey S, Yu, Jing, Mahdi, Akeel A, Lloyd, Robert G
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Circular DNA Crystal structure Data processing Dimerization DNA helicase DNA Helicases - genetics DNA, Circular - metabolism DNA-binding protein Enzymes Escherichia coli Escherichia coli - genetics Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Gene Deletion Genome Integrity, Repair and homologous recombination Metabolism Models, Molecular Mutation Neisseria Plasmids - metabolism Protein Structure, Tertiary RecA protein
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