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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.coli.

The C-terminal domain of the UvrC protein (UvrC CTD) is essential for 5' incision in the prokaryotic nucleotide excision repair process. We have determined the three-dimensional structure of the UvrC CTD using heteronuclear NMR techniques. The structure shows two helix-hairpin-helix (HhH) motifs connected by a small connector helix. The UvrC CTD is shown to mediate structure-specific DNA binding. The domain binds to a single-stranded-double-stranded junction DNA, with a strong specificity towards looped duplex DNA that contains at least six unpaired bases per loop ("bubble DNA"). Using chemical shift perturbation experiments, the DNA-binding surface is mapped to the first hairpin region encompassing the conserved glycine-valine-glycine residues followed by lysine-arginine-arginine, a positively charged surface patch and the second hairpin region consisting of glycine-isoleucine-serine. A model for the protein-DNA complex is proposed that accounts for this specificity.[1]

References

  1. Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.coli. Singh, S., Folkers, G.E., Bonvin, A.M., Boelens, R., Wechselberger, R., Niztayev, A., Kaptein, R. EMBO J. (2002) [Pubmed]
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