6DCR

E. coli PriA helicase winged helix domain deletion protein

Summary for 6DCR

• Entry DOI: 10.2210/pdb6dcr/pdb
• Related: 4NL4 4NL8
• Descriptor: Primosomal protein N', ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: pria, helicase, dna replication restart, dna binding protein
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 2
• Total formula weight: 155595.14

Authors

Satyshur, K.A.,Windgassen, T.A.,Keck, J.L. (deposition date: 2018-05-08, release date: 2018-09-05, Last modification date: 2023-10-11)

Primary citation

Windgassen, T.A.,Leroux, M.,Satyshur, K.A.,Sandler, S.J.,Keck, J.L.
Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.
Proc. Natl. Acad. Sci. U.S.A., 115:E9075-E9084, 2018

PubMed Abstract: DNA replication restart, the essential process that reinitiates prematurely terminated genome replication reactions, relies on exquisitely specific recognition of abandoned DNA replication-fork structures. The PriA DNA helicase mediates this process in bacteria through mechanisms that remain poorly defined. We report the crystal structure of a PriA/replication-fork complex, which resolves leading-strand duplex DNA bound to the protein. Interaction with PriA unpairs one end of the DNA and sequesters the 3'-most nucleotide from the nascent leading strand into a conserved protein pocket. Cross-linking studies reveal a surface on the winged-helix domain of PriA that binds to parental duplex DNA. Deleting the winged-helix domain alters PriA's structure-specific DNA unwinding properties and impairs its activity in vivo. Our observations lead to a model in which coordinated parental-, leading-, and lagging-strand DNA binding provide PriA with the structural specificity needed to act on abandoned DNA replication forks.

PubMed: 30201718
DOI: 10.1073/pnas.1809842115

Experimental method

X-RAY DIFFRACTION (1.978 Å)