8h1p
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == 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> | <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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.48Å</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> | </table> | ||
== Function == | == Function == | ||
| Line 10: | Line 11: | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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- | + | 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-oligomerisation 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-oligomerisation has remained elusive. In this 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. |
| - | 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 | + | 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 Mar;13(3):408-418. doi: 10.1002/2211-5463.13565. Epub 2023 , Feb 9. PMID:36707939<ref>PMID:36707939</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Cryo-EM structure of the human RAD52 protein
| |||||||||||
