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| | <StructureSection load='5jrb' size='340' side='right'caption='[[5jrb]], [[Resolution|resolution]] 2.41Å' scene=''> | | <StructureSection load='5jrb' size='340' side='right'caption='[[5jrb]], [[Resolution|resolution]] 2.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jrb]] 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=5JRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JRB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jrb]] 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=5JRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JRB 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]] 2.405Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jrb OCA], [http://pdbe.org/5jrb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jrb RCSB], [http://www.ebi.ac.uk/pdbsum/5jrb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jrb 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=5jrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jrb OCA], [https://pdbe.org/5jrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jrb RCSB], [https://www.ebi.ac.uk/pdbsum/5jrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jrb ProSAT]</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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kagawa, W]] | + | [[Category: Kagawa W]] |
| - | [[Category: Kurumizaka, H]] | + | [[Category: Kurumizaka H]] |
| - | [[Category: Saito, K]] | + | [[Category: Saito K]] |
| - | [[Category: Saotome, M]] | + | [[Category: Saotome M]] |
| - | [[Category: Dna annealing protein]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Multimeric ring formation]]
| + | |
| - | [[Category: Ssdna binding]]
| + | |
| Structural highlights
Function
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.[1]
Publication Abstract from PubMed
The Rad52 protein is a eukaryotic single-strand DNA-annealing protein that is involved in the homologous recombinational repair of DNA double-strand breaks. The isolated N-terminal half of the human RAD52 protein (RAD52(1-212)) forms an undecameric ring structure with a surface that is mostly positively charged. In the present study, it was found that RAD52(1-212) containing alanine mutations of the charged surface residues (Lys102, Lys133 and Glu202) is highly amenable to crystallization. The structure of the mutant RAD52(1-212) was solved at 2.4 A resolution. The structure revealed an association between the symmetry-related RAD52(1-212) rings, in which a partially unfolded, C-terminal region of RAD52 extended into the DNA-binding groove of the neighbouring ring in the crystal. The alanine mutations probably reduced the surface entropy of the RAD52(1-212) ring and stabilized the ring-ring association observed in the crystal.
Structure of the human DNA-repair protein RAD52 containing surface mutations.,Saotome M, Saito K, Onodera K, Kurumizaka H, Kagawa W Acta Crystallogr F Struct Biol Commun. 2016 Aug;72(Pt 8):598-603. doi:, 10.1107/S2053230X1601027X. Epub 2016 Jul 13. PMID:27487923[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kitao H, Yuan ZM. Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation. J Biol Chem. 2002 Dec 13;277(50):48944-8. Epub 2002 Oct 11. PMID:12379650 doi:10.1074/jbc.M208151200
- ↑ Saotome M, Saito K, Onodera K, Kurumizaka H, Kagawa W. Structure of the human DNA-repair protein RAD52 containing surface mutations. Acta Crystallogr F Struct Biol Commun. 2016 Aug;72(Pt 8):598-603. doi:, 10.1107/S2053230X1601027X. Epub 2016 Jul 13. PMID:27487923 doi:http://dx.doi.org/10.1107/S2053230X1601027X
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