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9WN8

Cryo-EM structure of the Retron-Eco8 complex in the presence of ATP

Summary for 9WN8
Entry DOI10.2210/pdb9wn8/pdb
EMDB information66110
DescriptorRetron Eco8 reverse transcriptase, Retron Eco8 OLD nuclease, RNA (83-MER), ... (4 entities in total)
Functional Keywordsrna binding protein, structural protein, antiviral protein, antiviral protein-rna-dna complex, antiviral protein/rna/dna
Biological sourceEscherichia coli
More
Total number of polymer chains16
Total formula weight721738.54
Authors
Zhang, J.T.,Ji, C.G.,Jia, N. (deposition date: 2025-09-04, release date: 2026-07-01, Last modification date: 2026-08-05)
Primary citationJi, C.G.,Li, Z.,Wei, X.Y.,Li, Y.,Zhang, J.T.,Liu, X.,Jia, N.
Mechanistic insights into activation of bacterial Retron-Eco8 immunity by phage protein SSB.
Nat Commun, 17:-, 2026
Cited by
PubMed Abstract: The Retron-Eco8 system, comprising a reverse transcriptase (RT), a non-coding RNA (ncRNA), and an OLD-family nuclease effector, protects bacteria from phage infection via abortive infection upon sensing a phage single-stranded DNA-binding protein (SSB). However, the molecular basis of this immunity remained unclear. Here, we report cryo-electron microscopy (cryo-EM) structures of Retron-Eco8 in inactive and activated states, revealing mechanisms of phage-triggered activation and effector function. Retron-Eco8 assembles into a tetrameric complex in which each protomer contains an RT, msrRNA-msdDNA duplex, and effector in an autoinhibited conformation. Upon phage infection, phage SSB binds msdDNA, relieving autoinhibition and activating the nuclease effector to degrade both phage and host DNA, triggering cell death to block phage propagation. Host SSB fails to activate the system, while DNA binding and oligomerization of phage SSB are essential for this activation, highlighting its specificity. These findings elucidate the molecular mechanism of Retron-Eco8-mediated immunity, facilitating retron-based biotechnological applications.
PubMed: 42270618
DOI: 10.1038/s41467-026-74106-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.81 Å)
Structure validation

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