1kn0: Difference between revisions

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<StructureSection load='1kn0' size='340' side='right'caption='[[1kn0]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='1kn0' size='340' side='right'caption='[[1kn0]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1kn0]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KN0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KN0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1kn0]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KN0 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rad52 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.85&#8491;</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=1kn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kn0 OCA], [http://pdbe.org/1kn0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1kn0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kn0 ProSAT], [http://www.topsan.org/Proteins/RSGI/1kn0 TOPSAN]</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=1kn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kn0 OCA], [https://pdbe.org/1kn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1kn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kn0 ProSAT], [https://www.topsan.org/Proteins/RSGI/1kn0 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RAD52_HUMAN RAD52_HUMAN]] Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.<ref>PMID:12379650</ref>
[https://www.uniprot.org/uniprot/RAD52_HUMAN RAD52_HUMAN] Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.<ref>PMID:12379650</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=1kn0 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=1kn0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a beta-beta-beta-alpha fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the beta-beta-beta-alpha fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.
Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form.,Kagawa W, Kurumizaka H, Ishitani R, Fukai S, Nureki O, Shibata T, Yokoyama S Mol Cell. 2002 Aug;10(2):359-71. PMID:12191481<ref>PMID:12191481</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kn0" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fukai, S]]
[[Category: Fukai S]]
[[Category: Ishitani, R]]
[[Category: Ishitani R]]
[[Category: Kagawa, W]]
[[Category: Kagawa W]]
[[Category: Kurumizaka, H]]
[[Category: Kurumizaka H]]
[[Category: Nureki, O]]
[[Category: Nureki O]]
[[Category: Structural genomic]]
[[Category: Shibata T]]
[[Category: Shibata, T]]
[[Category: Yokoyama S]]
[[Category: Yokoyama, S]]
[[Category: Beta-beta-beta-alpha fold]]
[[Category: Dna binding protein]]
[[Category: Dna-binding protein]]
[[Category: Ring protein]]
[[Category: Rsgi]]

Latest revision as of 13:25, 13 March 2024

Crystal Structure of the human Rad52 protein

1kn0, resolution 2.85Å

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