8a93

Complex of RecF-RecR-DNA from Thermus thermophilus.

spinqualitylabelsall models 8a93, resolution 3.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8a93 is a 7 chain structure with sequence from Thermus thermophilus HB8 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.05Å Ligands: ANP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5SLM9_THET8 The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.[HAMAP-Rule:MF_00365] Publication Abstract from PubMed 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. Mechanism of RecF-RecO-RecR cooperation in bacterial homologous recombination.,Nirwal S, Czarnocki-Cieciura M, Chaudhary A, Zajko W, Skowronek K, Chamera S, Figiel M, Nowotny M Nat Struct Mol Biol. 2023 May;30(5):650-660. doi: 10.1038/s41594-023-00967-z. , Epub 2023 Apr 20. PMID:37081315 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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