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1kft
From Proteopedia
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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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| - | [[Image:1kft.gif|left|200px]]<br /><applet load="1kft" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | 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== |
| - | The C-terminal domain of the UvrC protein (UvrC CTD) is essential for 5' | + | <StructureSection load='1kft' size='340' side='right'caption='[[1kft]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1kft]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFT FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kft OCA], [https://pdbe.org/1kft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kft RCSB], [https://www.ebi.ac.uk/pdbsum/1kft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kft ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/UVRC_ECOLI 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.<ref>PMID:1387639</ref> <ref>PMID:10671556</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kf/1kft_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kft ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:12426397</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1kft" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[UvrABC 3D structures|UvrABC 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Boelens R]] | ||
| + | [[Category: Bonvin AMJJ]] | ||
| + | [[Category: Folkers GE]] | ||
| + | [[Category: Kaptein R]] | ||
| + | [[Category: Niztayev A]] | ||
| + | [[Category: Singh S]] | ||
| + | [[Category: Wechselberger R]] | ||
Current revision
Solution Structure of the C-Terminal domain of UvrC from E-coli
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