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{{STRUCTURE_1t5l|  PDB=1t5l  |  SCENE=  }}
===Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2===
{{ABSTRACT_PUBMED_15192705}}


==Function==
==Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2==
[[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]  
<StructureSection load='1t5l' size='340' side='right'caption='[[1t5l]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1t5l]] is a 2 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=1T5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T5L FirstGlance]. <br>
[[1t5l]] is a 2 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=1T5L OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1t5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t5l OCA], [https://pdbe.org/1t5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t5l RCSB], [https://www.ebi.ac.uk/pdbsum/1t5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t5l ProSAT]</span></td></tr>
</table>
== Function ==
[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]
== 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/t5/1t5l_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=1t5l ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[UvrABC|UvrABC]]
*[[UvrABC|UvrABC]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:015192705</ref><references group="xtra"/><references/>
[[Category: Large Structures]]
[[Category: Bacillus caldotenax]]
[[Category: Croteau DL]]
[[Category: Croteau, D L.]]
[[Category: DellaVecchia MJ]]
[[Category: DellaVecchia, M J.]]
[[Category: Kisker C]]
[[Category: Houten, B Van.]]
[[Category: Mandavilli BS]]
[[Category: Kisker, C.]]
[[Category: Skorvaga M]]
[[Category: Mandavilli, B S.]]
[[Category: Theis K]]
[[Category: Skorvaga, M.]]
[[Category: Truglio JJ]]
[[Category: Theis, K.]]
[[Category: Van Houten B]]
[[Category: Truglio, J J.]]
[[Category: Dna damage]]
[[Category: Dna excision repair]]
[[Category: Dna repair]]
[[Category: Mfd]]
[[Category: Ner]]
[[Category: Nucleotide excision repair]]
[[Category: Trcf]]
[[Category: Uvra]]
[[Category: Uvrb]]
[[Category: Uvrc]]

Latest revision as of 11:36, 14 February 2024

Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2

Structural highlights

1t5l is a 2 chain structure with sequence from Bacillus caldotenax. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1t5l, resolution 2.60Å

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