View source for 8oel


==Condensed RPA-DNA nucleoprotein filament==
<StructureSection load='8oel' size='340' side='right'caption='[[8oel]], [[Resolution|resolution]] 8.24&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8oel]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OEL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.24&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=8oel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8oel OCA], [https://pdbe.org/8oel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8oel RCSB], [https://www.ebi.ac.uk/pdbsum/8oel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8oel ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G8ZHS0_PYRAB G8ZHS0_PYRAB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Replication Protein A (RPA) is a heterotrimeric single stranded DNA-binding protein with essential roles in DNA replication, recombination and repair. Little is known about the structure of RPA in Archaea, the third domain of life. By using an integrative structural, biochemical and biophysical approach, we extensively characterize RPA from Pyrococcus abyssi in the presence and absence of DNA. The obtained X-ray and cryo-EM structures reveal that the trimerization core and interactions promoting RPA clustering on ssDNA are shared between archaea and eukaryotes. However, we also identified a helical domain named AROD (Acidic Rpa1 OB-binding Domain), and showed that, in Archaea, RPA forms an unanticipated tetrameric supercomplex in the absence of DNA. The four RPA molecules clustered within the tetramer could efficiently coat and protect stretches of ssDNA created by the advancing replisome. Finally, our results provide insights into the evolution of this primordial replication factor in eukaryotes.

DNA-binding mechanism and evolution of replication protein A.,Madru C, Martinez-Carranza M, Laurent S, Alberti AC, Chevreuil M, Raynal B, Haouz A, Le Meur RA, Delarue M, Henneke G, Flament D, Krupovic M, Legrand P, Sauguet L Nat Commun. 2023 Apr 22;14(1):2326. doi: 10.1038/s41467-023-38048-w. PMID:37087464<ref>PMID:37087464</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8oel" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Pyrococcus abyssi]]
[[Category: Madru C]]
[[Category: Martinez-Carranza M]]
[[Category: Sauguet L]]