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9E90

Ec83 Retron PtuA/PtuB (2-1) complex bound to ATP

Summary for 9E90
Entry DOI10.2210/pdb9e90/pdb
EMDB information47738
DescriptorRetron Ec83 putative HNH endonuclease, Retron Ec83 probable ATPase, ZINC ION, ... (4 entities in total)
Functional Keywordsatpase, retron, antiviral protein, dimer
Biological sourceEscherichia coli
More
Total number of polymer chains3
Total formula weight154848.90
Authors
Rish, A.D.,Wang, C.,Fu, T.M. (deposition date: 2024-11-06, release date: 2025-07-02, Last modification date: 2025-09-03)
Primary citationWang, C.,Rish, A.D.,Armbruster, E.G.,Xie, J.,Loveland, A.B.,Shen, Z.,Gu, B.,Korostelev, A.A.,Pogliano, J.,Fu, T.M.
Disassembly activates Retron-Septu for antiphage defense.
Science, 389:eadv3344-eadv3344, 2025
Cited by
PubMed Abstract: Retrons are antiphage defense systems that produce multicopy single-stranded DNA (msDNA) and hold promises for genome engineering. However, the mechanisms of defense remain unclear. The Retron-Septu system uniquely integrates retron and Septu antiphage defenses. Cryo-electron microscopy structures reveal asymmetric nucleoprotein complexes comprising a reverse transcriptase (RT), msDNA (a hybrid of msdDNA and msrRNA), and two PtuAB copies. msdDNA and msrRNA are essential for assembling this complex, with msrRNA adopting a conserved lariat-like structure that regulates reverse transcription. Notably, the assembled Retron-Septu complex is inactive, with msdDNA occupying the PtuA DNA-binding site. Activation occurs upon disassembly, releasing PtuAB, which degrades single-stranded DNA to restrict phage replication. This "arrest-and-release" mechanism underscores the dynamic regulatory roles of msDNA, advancing our understanding of antiphage defense strategies.
PubMed: 40504952
DOI: 10.1126/science.adv3344
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.45 Å)
Structure validation

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