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==DNA replication fork binding triggers structural changes in the PriA DNA helicase that regulate the PriA-PriB replication restart pathway in E. coli==
<StructureSection load='8fak' size='340' side='right'caption='[[8fak]], [[Resolution|resolution]] 3.22&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8fak]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] 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=8FAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FAK 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]] 3.22&#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=8fak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fak OCA], [https://pdbe.org/8fak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fak RCSB], [https://www.ebi.ac.uk/pdbsum/8fak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fak ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRIB_ECOLI PRIB_ECOLI] Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT.<ref>PMID:1856227</ref> <ref>PMID:1646811</ref> <ref>PMID:8366072</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial replisomes often dissociate from replication forks before chromosomal replication is complete. To avoid the lethal consequences of such situations, bacteria have evolved replication restart pathways that reload replisomes onto prematurely terminated replication forks. To understand how the primary replication restart pathway in E. coli (PriA-PriB) selectively acts on replication forks, we determined the cryogenic-electron microscopy structure of a PriA/PriB/replication fork complex. Replication fork specificity arises from extensive PriA interactions with each arm of the branched DNA. These interactions reshape the PriA protein to create a pore encircling single-stranded lagging-strand DNA while also exposing a surface of PriA onto which PriB docks. Together with supporting biochemical and genetic studies, the structure reveals a switch-like mechanism for replication restart initiation in which restructuring of PriA directly couples replication fork recognition to PriA/PriB complex formation to ensure robust and high-fidelity replication re-initiation.

Replication fork binding triggers structural changes in the PriA helicase that govern DNA replication restart in E. coli.,Duckworth AT, Ducos PL, McMillan SD, Satyshur KA, Blumenthal KH, Deorio HR, Larson JA, Sandler SJ, Grant T, Keck JL Nat Commun. 2023 May 11;14(1):2725. doi: 10.1038/s41467-023-38144-x. PMID:37169801<ref>PMID:37169801</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8fak" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Blumenthal KH]]
[[Category: Deorio HR]]
[[Category: Duckworth AT]]
[[Category: Ducos PL]]
[[Category: Grant T]]
[[Category: Keck JL]]
[[Category: Larson JA]]
[[Category: McMillan SD]]
[[Category: Sandler SJ]]
[[Category: Satyshur KA]]