1kft
From Proteopedia
(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 ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1kft.gif|left|200px]]<br /><applet load="1kft" size=" | + | [[Image:1kft.gif|left|200px]]<br /><applet load="1kft" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kft" /> | caption="1kft" /> | ||
'''Solution Structure of the C-Terminal domain of UvrC from E-coli'''<br /> | '''Solution Structure of the C-Terminal domain of UvrC from E-coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The C-terminal domain of the UvrC protein (UvrC CTD) is essential for 5' | + | 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== | ==About this Structure== | ||
| - | 1KFT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1KFT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFT OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Boelens, R.]] | [[Category: Boelens, R.]] | ||
| - | [[Category: Bonvin, A | + | [[Category: Bonvin, A M.J J.]] |
| - | [[Category: Folkers, G | + | [[Category: Folkers, G E.]] |
[[Category: Kaptein, R.]] | [[Category: Kaptein, R.]] | ||
[[Category: Niztayev, A.]] | [[Category: Niztayev, A.]] | ||
| Line 24: | Line 24: | ||
[[Category: hhh domain]] | [[Category: hhh domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:40 2008'' |
Revision as of 11:33, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 13:33:40 2008
