4NL8

PriA Helicase Bound to SSB C-terminal Tail Peptide

Summary for 4NL8

• Entry DOI: 10.2210/pdb4nl8/pdb
• Related: 2D7E 2D7G 2D7H 2DWL 2DWM 2DWN 4NL4
• Descriptor: Single-stranded DNA-binding protein, Primosome assembly protein PriA, ZINC ION (3 entities in total)
• Functional Keywords: pria, ssb c-terminal peptide, reca fold, winged helix domain, helicase, dna binding protein
• Biological source: Klebsiella pneumoniae subsp. pneumoniae; More
• Total number of polymer chains: 6
• Total formula weight: 254005.26

Authors

Bhattacharyya, B.,George, N.P.,Thurmes, T.M.,Keck, J.L. (deposition date: 2013-11-13, release date: 2014-01-08, Last modification date: 2024-02-28)

Primary citation

Bhattacharyya, B.,George, N.P.,Thurmes, T.M.,Zhou, R.,Jani, N.,Wessel, S.R.,Sandler, S.J.,Ha, T.,Keck, J.L.
Structural mechanisms of PriA-mediated DNA replication restart.
Proc.Natl.Acad.Sci.USA, 111:1373-1378, 2014

PubMed Abstract: Collisions between cellular DNA replication machinery (replisomes) and damaged DNA or immovable protein complexes can dissociate replisomes before the completion of replication. This potentially lethal problem is resolved by cellular "replication restart" reactions that recognize the structures of prematurely abandoned replication forks and mediate replisomal reloading. In bacteria, this essential activity is orchestrated by the PriA DNA helicase, which identifies replication forks via structure-specific DNA binding and interactions with fork-associated ssDNA-binding proteins (SSBs). However, the mechanisms by which PriA binds replication fork DNA and coordinates subsequent replication restart reactions have remained unclear due to the dearth of high-resolution structural information available for the protein. Here, we describe the crystal structures of full-length PriA and PriA bound to SSB. The structures reveal a modular arrangement for PriA in which several DNA-binding domains surround its helicase core in a manner that appears to be poised for binding to branched replication fork DNA structures while simultaneously allowing complex formation with SSB. PriA interaction with SSB is shown to modulate SSB/DNA complexes in a manner that exposes a potential replication initiation site. From these observations, a model emerges to explain how PriA links recognition of diverse replication forks to replication restart.

PubMed: 24379377
DOI: 10.1073/pnas.1318001111

Experimental method

X-RAY DIFFRACTION (4.08 Å)