8h1p: Difference between revisions

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'''Unreleased structure'''


The entry 8h1p is ON HOLD  until Paper Publication
==Cryo-EM structure of the human RAD52 protein==
<StructureSection load='8h1p' size='340' side='right'caption='[[8h1p]], [[Resolution|resolution]] 3.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8h1p]] 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=8H1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H1P FirstGlance]. <br>
</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=8h1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h1p OCA], [https://pdbe.org/8h1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h1p RCSB], [https://www.ebi.ac.uk/pdbsum/8h1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h1p ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== Publication Abstract from PubMed ==
The human RAD52 protein, which forms an oligomeric ring structure, is involved in DNA double-strand break repair. The N-terminal half of RAD52 is primarily responsible for self-oligomerization and DNA binding. Crystallographic studies have revealed the detailed structure of the N-terminal half. However, only low-resolution structures have been reported for the full-length protein, and thus the structural role of the C-terminal half in self-oligomerization has remained elusive. In the present study, we determined the solution structure of the human RAD52 protein by cryo-electron microscopy (cryo-EM), at an average resolution of 3.5 A. The structure revealed an undecameric ring that is nearly identical to the crystal structures of the N-terminal half. The cryo-EM map for the C-terminal half was poorly defined, indicating that the region is intrinsically disordered. The present cryo-EM structure provides important insights into the mechanistic roles played by the N-terminal and C-terminal halves of RAD52 during DNA double-strand break repair.


Authors:  
The cryo-EM structure of full-length RAD52 protein contains an undecameric ring.,Kinoshita C, Takizawa Y, Saotome M, Ogino S, Kurumizaka H, Kagawa W FEBS Open Bio. 2023 Jan 27. doi: 10.1002/2211-5463.13565. PMID:36707939<ref>PMID:36707939</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8h1p" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kagawa W]]
[[Category: Kinoshita C]]
[[Category: Kurumizaka H]]
[[Category: Ogino S]]
[[Category: Saotome M]]
[[Category: Takizawa Y]]
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