1KFT

Solution Structure of the C-Terminal domain of UvrC from E-coli

Summary for 1KFT

• Entry DOI: 10.2210/pdb1kft/pdb
• NMR Information: BMRB: 5217
• Descriptor: Excinuclease ABC subunit C (1 entity in total)
• Functional Keywords: helix-hairpin-helix, hhh domain, dna-binding domain, dna binding protein
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P07028
• Total number of polymer chains: 1
• Total formula weight: 8579.86

Authors

Singh, S.,Folkers, G.E.,Bonvin, A.M.J.J.,Boelens, R.,Wechselberger, R.,Niztayev, A.,Kaptein, R. (deposition date: 2001-11-23, release date: 2002-11-20, Last modification date: 2024-05-29)

Primary citation

Singh, S.,Folkers, G.E.,Bonvin, A.M.J.J.,Boelens, R.,Wechselberger, R.,Niztayev, A.,Kaptein, R.
Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.coli
EMBO J., 21:6257-6266, 2002

PubMed 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-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.

PubMed: 12426397
DOI: 10.1093/emboj/cdf627

Experimental method

SOLUTION NMR