8FAK

DNA replication fork binding triggers structural changes in the PriA DNA helicase that regulate the PriA-PriB replication restart pathway in E. coli

This is a non-PDB format compatible entry.

Summary for 8FAK

• Entry DOI: 10.2210/pdb8fak/pdb
• EMDB information: 28959
• Descriptor: Primosomal replication protein N, DNA (5'-D(P*CP*AP*GP*AP*CP*TP*CP*AP*TP*TP*TP*AP*GP*CP*CP*CP*TP*TP*AP*TP*CP*CP*G)-3'), Primosomal protein N', ... (6 entities in total)
• Functional Keywords: pria, prib, replication restart, e. coli, helicase-dna complex, helicase/dna
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 6
• Total formula weight: 133989.76

Authors

Duckworth, A.T.,Ducos, P.L.,McMillan, S.D.,Satyshur, K.A.,Blumenthal, K.H.,Deorio, H.R.,Larson, J.A.,Sandler, S.J.,Grant, T.,Keck, J.L. (deposition date: 2022-11-28, release date: 2023-05-10, Last modification date: 2024-10-23)

Primary citation

Duckworth, A.T.,Ducos, P.L.,McMillan, S.D.,Satyshur, K.A.,Blumenthal, K.H.,Deorio, H.R.,Larson, J.A.,Sandler, S.J.,Grant, T.,Keck, J.L.
Replication fork binding triggers structural changes in the PriA helicase that govern DNA replication restart in E. coli.
Nat Commun, 14:2725-2725, 2023

PubMed Abstract: 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.

PubMed: 37169801
DOI: 10.1038/s41467-023-38144-x

Experimental method

ELECTRON MICROSCOPY (3.22 Å)