9ZBT

Visualization of PriA/PriB/DnaT complexes reveals mechanisms governing structure-specific assembly of the DNA replication restart primosome

This is a non-PDB format compatible entry.

Summary for 9ZBT

• Entry DOI: 10.2210/pdb9zbt/pdb
• EMDB information: 74008
• Descriptor: Replication restart protein DnaT, Replication restart protein PriB, DNA (33-MER), ... (7 entities in total)
• Functional Keywords: dna replication, helicase, oligomer, dna repair, replication
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 7
• Total formula weight: 153463.79

Authors

Duckworth, A.T.,Keck, J.L.,Grant, T. (deposition date: 2025-11-21, release date: 2026-05-27)

Primary citation

Ducos, P.L.,Duckworth, A.T.,Satyshur, K.A.,Keck, J.L.,Grant, T.
Visualization of the complete preprimosome reveals the structural mechanisms governing DNA replication restart.
Nat Commun, 2026

PubMed Abstract: Replication restart pathways reinitiate DNA replication processes following their premature termination. In Escherichia coli, this essential process begins with regulated assembly of the preprimosome complex, comprising the PriA, PriB, and DnaT proteins, onto an abandoned replication fork. Here, we present two distinct preprimosome structures. One represents an intermediate stage in preprimosome assembly with a single DnaT C-terminal domain (DnaT) bound to PriA/PriB/DNA. The second captures the mature preprimosome, in which filamentation of multiple DnaT molecules catalyzes the handoff of the single-stranded lagging-strand DNA from PriB to DnaT. The DnaT N-terminal domain forms a separate, independent oligomer in the mature structure. Taken together, our results detail the molecular mechanisms underlying replication restart initiation and regulation and suggest mechanistic similarities between DnaT and the canonical initiator protein DnaA.

PubMed: 42140935
DOI: 10.1038/s41467-026-73239-1

Experimental method

ELECTRON MICROSCOPY (3.22 Å)