Structural highlights
Function
[UVRC_ECOLI] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.coli.,Singh S, Folkers GE, Bonvin AM, Boelens R, Wechselberger R, Niztayev A, Kaptein R EMBO J. 2002 Nov 15;21(22):6257-66. PMID:12426397[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lin JJ, Sancar A. Active site of (A)BC excinuclease. I. Evidence for 5' incision by UvrC through a catalytic site involving Asp399, Asp438, Asp466, and His538 residues. J Biol Chem. 1992 Sep 5;267(25):17688-92. PMID:1387639
- ↑ Verhoeven EE, van Kesteren M, Moolenaar GF, Visse R, Goosen N. Catalytic sites for 3' and 5' incision of Escherichia coli nucleotide excision repair are both located in UvrC. J Biol Chem. 2000 Feb 18;275(7):5120-3. PMID:10671556
- ↑ Singh S, Folkers GE, Bonvin AM, 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. 2002 Nov 15;21(22):6257-66. PMID:12426397
