2fdc: Difference between revisions

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<StructureSection load='2fdc' size='340' side='right'caption='[[2fdc]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='2fdc' size='340' side='right'caption='[[2fdc]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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>
</td></tr><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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1t5l|1t5l]], [[1d9x|1d9x]], [[1d9z|1d9z]], [[1yd1|1yd1]], [[1qoj|1qoj]]</div></td></tr>
<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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uvrB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1395 'Bacillus caldotenax'])</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=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>
<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>
</table>
</table>
== Function ==
== 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]  
[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 ==
== 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=2fdc 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=2fdc ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DNA-damage recognition in the nucleotide excision repair (NER) cascade is a complex process, operating on a wide variety of damages. UvrB is the central component in prokaryotic NER, directly involved in DNA-damage recognition and guiding the DNA through repair synthesis. We report the first structure of a UvrB-double-stranded DNA complex, providing insights into the mechanism by which UvrB binds DNA, leading to formation of the preincision complex. One DNA strand, containing a 3' overhang, threads behind a beta-hairpin motif of UvrB, indicating that this motif inserts between the strands of the double helix, thereby locking down either the damaged or undamaged strand. The nucleotide directly behind the beta-hairpin is flipped out and inserted into a small, highly conserved pocket in UvrB.
Structural basis for DNA recognition and processing by UvrB.,Truglio JJ, Karakas E, Rhau B, Wang H, DellaVecchia MJ, Van Houten B, Kisker C Nat Struct Mol Biol. 2006 Apr;13(4):360-4. Epub 2006 Mar 12. PMID:16532007<ref>PMID:16532007</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fdc" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[UvrABC|UvrABC]]
*[[UvrABC|UvrABC]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus caldotenax]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kisker, C]]
[[Category: Kisker C]]
[[Category: Truglio, J J]]
[[Category: Truglio JJ]]
[[Category: Dna binding protein-dna complex]]
[[Category: Dna repair]]
[[Category: Ner]]
[[Category: Nucleotide excision repair]]
[[Category: Protein-dna complex]]
[[Category: Uvra]]
[[Category: Uvrb]]
[[Category: Uvrc]]
[[Category: Uvrd]]

Latest revision as of 12:22, 14 February 2024

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

Structural highlights

2fdc is a 4 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 3.3Å
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

2fdc, resolution 3.30Å

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