1kft
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(New page: 200px<br /><applet load="1kft" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kft" /> '''Solution Structure of the C-Terminal domain ...)
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Revision as of 17:03, 20 November 2007
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Solution Structure of the C-Terminal domain of UvrC from E-coli
Overview
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.
About this Structure
1KFT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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