Abstract
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-specificity 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.
Original language | Undefined/Unknown |
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Pages (from-to) | 6257-6266 |
Number of pages | 10 |
Journal | EMBO Journal |
Volume | 21 |
Issue number | 22 |
DOIs | |
Publication status | Published - 2002 |