View source for 1kft


==Solution Structure of the C-Terminal domain of UvrC from E-coli==
<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].
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== 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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1kft" style="background-color:#fffaf0;"></div>

==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]]