8AB0

Complex of RecO-RecR-DNA from Thermus thermophilus.

Summary for 8AB0

• Entry DOI: 10.2210/pdb8ab0/pdb
• Related: 8A8J 8A93 8BPR
• EMDB information: 15231 15267 15308 16164
• Descriptor: Recombination protein RecR, DNA repair protein RecO, Oligo1, ... (5 entities in total)
• Functional Keywords: dna binding protein, dna repair pathway, recfor pathway, thermus thermophilus
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 7
• Total formula weight: 130476.05

Authors

Nirwal, S.,Czarnocki-Cieciura, M.,Chaudhary, A.,Zajko, W.,Skowronek, K.,Chamera, S.,Figiel, M.,Nowotny, M. (deposition date: 2022-07-04, release date: 2023-04-26, Last modification date: 2024-07-24)

Primary citation

Nirwal, S.,Czarnocki-Cieciura, M.,Chaudhary, A.,Zajko, W.,Skowronek, K.,Chamera, S.,Figiel, M.,Nowotny, M.
Mechanism of RecF-RecO-RecR cooperation in bacterial homologous recombination.
Nat.Struct.Mol.Biol., 30:650-660, 2023

PubMed Abstract: In bacteria, one type of homologous-recombination-based DNA-repair pathway involves RecFOR proteins that bind at the junction between single-stranded (ss) and double-stranded (ds) DNA. They facilitate the replacement of SSB protein, which initially covers ssDNA, with RecA, which mediates the search for homologous sequences. However, the molecular mechanism of RecFOR cooperation remains largely unknown. We used Thermus thermophilus proteins to study this system. Here, we present a cryo-electron microscopy structure of the RecF-dsDNA complex, and another reconstruction that shows how RecF interacts with two different regions of the tetrameric RecR ring. Lower-resolution reconstructions of the RecR-RecO subcomplex and the RecFOR-DNA assembly explain how RecO is positioned to interact with ssDNA and SSB, which is proposed to lock the complex on a ssDNA-dsDNA junction. Our results integrate the biochemical data available for the RecFOR system and provide a framework for its complete understanding.

PubMed: 37081315
DOI: 10.1038/s41594-023-00967-z

Experimental method

ELECTRON MICROSCOPY (6.09 Å)