8aas

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'''Unreleased structure'''
 
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The entry 8aas is ON HOLD until Paper Publication
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==Crystal structure of the Pyrococcus abyssi RPA trimerization core bound to poly-dT20 ssDNA==
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<StructureSection load='8aas' size='340' side='right'caption='[[8aas]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8aas]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi_GE5 Pyrococcus abyssi GE5] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AAS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8aas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aas OCA], [https://pdbe.org/8aas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aas RCSB], [https://www.ebi.ac.uk/pdbsum/8aas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aas ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/G8ZHS0_PYRAB G8ZHS0_PYRAB]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8aas" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pyrococcus abyssi GE5]]
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[[Category: Synthetic construct]]
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[[Category: Legrand P]]
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[[Category: Madru C]]
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[[Category: Sauguet L]]

Revision as of 07:27, 3 May 2023

Crystal structure of the Pyrococcus abyssi RPA trimerization core bound to poly-dT20 ssDNA

PDB ID 8aas

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