1qoj: Difference between revisions

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<StructureSection load='1qoj' size='340' side='right'caption='[[1qoj]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1qoj' size='340' side='right'caption='[[1qoj]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qoj]] is a 2 chain structure with 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=1QOJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QOJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1qoj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOJ FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e52|1e52]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qoj OCA], [http://pdbe.org/1qoj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qoj RCSB], [http://www.ebi.ac.uk/pdbsum/1qoj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qoj ProSAT]</span></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=1qoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qoj OCA], [https://pdbe.org/1qoj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qoj RCSB], [https://www.ebi.ac.uk/pdbsum/1qoj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qoj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UVRB_ECOLI UVRB_ECOLI] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.<ref>PMID:12145219</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1qoj ConSurf].
</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=1qoj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A crystal structure of the C-terminal domain of Escherichia coli UvrB (UvrB') has been solved to 3.0 A resolution. The domain adopts a helix-loop-helix fold which is stabilised by the packing of hydrophobic side-chains between helices. From the UvrB' fold, a model for a domain of UvrC (UvrC') that has high sequence homology with UvrB' has been made. In the crystal, a dimerisation of UvrB domains is seen involving specific hydrophobic and salt bridge interactions between residues in and close to the loop region of the domain. It is proposed that a homologous mode of interaction may occur between UvrB and UvrC. This interaction is likely to be flexible, potentially spanning &gt; 50 A.
Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction.,Sohi M, Alexandrovich A, Moolenaar G, Visse R, Goosen N, Vernede X, Fontecilla-Camps JC, Champness J, Sanderson MR FEBS Lett. 2000 Jan 14;465(2-3):161-4. PMID:10631326<ref>PMID:10631326</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qoj" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[UvrABC|UvrABC]]
*[[UvrABC 3D structures|UvrABC 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Alexandrovich, A]]
[[Category: Alexandrovich A]]
[[Category: Champness, J]]
[[Category: Champness J]]
[[Category: Fontecilla-Camps, J]]
[[Category: Fontecilla-Camps J]]
[[Category: Goosen, N]]
[[Category: Goosen N]]
[[Category: Moolenaar, G]]
[[Category: Moolenaar G]]
[[Category: Sanderson, M R]]
[[Category: Sanderson MR]]
[[Category: Sohi, M]]
[[Category: Sohi M]]
[[Category: Vernede, X]]
[[Category: Vernede X]]
[[Category: Visse, R]]
[[Category: Visse R]]
[[Category: Dna excision repair]]
[[Category: Nucleotide excision repair]]
[[Category: Uvrb protein]]
[[Category: Uvrb-c interaction]]
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