2fdc

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{{STRUCTURE_2fdc| PDB=2fdc | SCENE= }}
 
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===Structural Basis of DNA Damage Recognition and Processing by UvrB: crystal structure of a UvrB/DNA complex===
 
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{{ABSTRACT_PUBMED_16532007}}
 
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==Function==
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==Structural Basis of DNA Damage Recognition and Processing by UvrB: crystal structure of a UvrB/DNA complex==
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[[http://www.uniprot.org/uniprot/UVRB_BACCA UVRB_BACCA]] 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 (By similarity).[HAMAP-Rule:MF_00204]
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<StructureSection load='2fdc' size='340' side='right'caption='[[2fdc]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2fdc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_caldotenax Bacillus caldotenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FDC FirstGlance]. <br>
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[[2fdc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_caldotenax Bacillus caldotenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FDC OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLQ:N-[6-(ACETYLAMINO)HEXYL]-3,6-DIHYDROXY-3-OXO-3H-SPIRO[2-BENZOFURAN-1,9-XANTHENE]-6-CARBOXAMIDE'>FLQ</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fdc OCA], [https://pdbe.org/2fdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fdc RCSB], [https://www.ebi.ac.uk/pdbsum/2fdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fdc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/UVRB_BACCA UVRB_BACCA] 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 (By similarity).[HAMAP-Rule:MF_00204]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fd/2fdc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2fdc ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
*[[UvrABC|UvrABC]]
*[[UvrABC|UvrABC]]
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:016532007</ref><references group="xtra"/><references/>
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[[Category: Large Structures]]
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[[Category: Bacillus caldotenax]]
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[[Category: Kisker C]]
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[[Category: Kisker, C.]]
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[[Category: Truglio JJ]]
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[[Category: Truglio, J J.]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Dna repair]]
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[[Category: Ner]]
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[[Category: Nucleotide excision repair]]
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[[Category: Protein-dna complex]]
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[[Category: Uvra]]
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[[Category: Uvrb]]
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[[Category: Uvrc]]
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[[Category: Uvrd]]
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Current revision

Structural Basis of DNA Damage Recognition and Processing by UvrB: crystal structure of a UvrB/DNA complex

PDB ID 2fdc

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