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Open data
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Basic information
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| Title | Cryo-EM structure of the Retron-Eco8-SSB complex | |||||||||
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Keywords | ANTIVIRAL PROTEIN/DNA/RNA / ANTIVIRAL PROTEIN-DNA-RNA complex | |||||||||
| Function / homology | Function and homology informationnuclease activity / RNA-directed DNA polymerase / RNA-directed DNA polymerase activity / defense response to virus / Hydrolases; Acting on ester bonds / ATP hydrolysis activity / RNA binding / ATP binding / metal ion binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.11 Å | |||||||||
Authors | Zhang JT / Ji CG / Li ZL / Wei XY / Jia N | |||||||||
| Funding support | 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: Mechanistic insights into activation of bacterial Retron-Eco8 immunity by phage protein SSB. Authors: Chao-Guang Ji / Zhuolin Li / Xin-Yang Wei / Yuelong Li / Jun-Tao Zhang / Xueyan Liu / Ning Jia / ![]() 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 ...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. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Header (meta data) | emd-69132-v30.xml emd-69132.xml | 19.1 KB 19.1 KB | Display Display | EMDB header |
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| Images | emd_69132.png | 62.9 KB | ||
| Map data | emd_69132.map.gz | 633 MB | EMDB map data format | |
| Masks | emd_69132_msk_1.map | 669.9 MB | Mask map | |
| Filedesc metadata | emd-69132.cif.gz | 6.6 KB | ||
| Others | emd_69132_half_map_1.map.gz emd_69132_half_map_2.map.gz | 620.9 MB 620.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-69132 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-69132 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 23orMC ![]() 9lbqC ![]() 9wn8C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
-Supplemental data
-Mask #1
| File | emd_69132_msk_1.map | ||||||||||||
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-Half map: #1
| File | emd_69132_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_69132_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Heterotetramer Retron-Eco8-SSB complex
| Entire | Name: Heterotetramer Retron-Eco8-SSB complex |
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| Components |
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-Supramolecule #1: Heterotetramer Retron-Eco8-SSB complex
| Supramolecule | Name: Heterotetramer Retron-Eco8-SSB complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Retron Eco8 reverse transcriptase
| Macromolecule | Name: Retron Eco8 reverse transcriptase / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: RNA-directed DNA polymerase |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 43.273203 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MKTKKMILVD KVFYEKILSV ESFKENIITQ SAIPKISNKE VRLISSGSKI FYAINNTSPH SHVQLRLNRF FLSHIPLNSA AKAFVRGGS YLKYLEPHIY GSSYCRLDIS SFFNNISFDD VKQSLSPYIK DEYLIGTEQK LIDAILNSVG YESPIRKDKG M IIPMGFRT ...String: MKTKKMILVD KVFYEKILSV ESFKENIITQ SAIPKISNKE VRLISSGSKI FYAINNTSPH SHVQLRLNRF FLSHIPLNSA AKAFVRGGS YLKYLEPHIY GSSYCRLDIS SFFNNISFDD VKQSLSPYIK DEYLIGTEQK LIDAILNSVG YESPIRKDKG M IIPMGFRT SPAISNIVFR KMDLLIQDFC AKKGVIYSRY ADDMLFSNPR ESKLLMSDYF IDEISSLLSI MGFNINQSKY IS REKEISI NGYVIENKGG NGSIGTIRLS KSKLNTVLKV THALAQNIPY KNICNKYIKV RLKEKNIKYE SKKDEFEKKY YRD QLINYL GGYRSYLISL VKFHSEYKCV NSDFIIQING ILNDIQNHIQ KIKKNRRL UniProtKB: Retron Eco8 reverse transcriptase |
-Macromolecule #2: Retron Eco8 OLD nuclease
| Macromolecule | Name: Retron Eco8 OLD nuclease / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO / EC number: Hydrolases; Acting on ester bonds |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 87.373789 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MTIESIRVKN LLSFDDVILR DFRDINCIIG RNNVGKSNLL KVIRYFYAKL ENKKVIPLDF HTNYNAVGEI TFTFDTTRIK KIVTSRKNN GRFHKHIYNT LFKSSSVKLN FEELIARKNS TNKSFFSLTL TICKDDSVMW SVDDPKVRSL LATLYPFLYI E TRHIDLYD ...String: MTIESIRVKN LLSFDDVILR DFRDINCIIG RNNVGKSNLL KVIRYFYAKL ENKKVIPLDF HTNYNAVGEI TFTFDTTRIK KIVTSRKNN GRFHKHIYNT LFKSSSVKLN FEELIARKNS TNKSFFSLTL TICKDDSVMW SVDDPKVRSL LATLYPFLYI E TRHIDLYD WNPIWKLISN LNSFNFDDVD HDELVNFLDE KISSRKGDYK KYIDRVVSVI DTKPYTYKEK VINYIKVAIK GD SFVNAGE ELFTQSDGTN SNKFLETLLH LLITLTRTEF ISPIVYIDEP EVGLHPKLAE SFVSNLNKIY SKFKKTSELS GPG RYKTPY PNIFYSTHSP SILKQTIKLF GKDQQVLHFS KKKDGSTRVN KINSTYSDER FLNIFSDNEA RLFFSEYIVF VEGA TELEL FRNLSLLNLY PAFSLADIYD ANEVILANIN PGYSKASIPF VIIKDIDTLI DYSIKTEKFS LRPLFEKMIK ELTKE FDYY DTGFGRVRKE IDLFSDIQSS TKKHMDSGLF FKRFSLHNLS SRINKVSRKL NRYFMTTTIE GALINEQSLP YFFNWI GDV ILTQMTINNP NPDKFIEAMR RRYNIKSQVV PLFKSVFCIG LNHPVYSSAV DKQALRIKLS FLNYLKRKVY SDFNNEK EI VLALRLAFGG KTETQYTLDK LRKDGEAELF REKIKNYKNN ELFFLEPQMT KTSGWVTTFL NYTIEKITSE ESDDDRIR Q KLSFIFPEII SIIEQASSSI EAEESSLTG UniProtKB: Retron Eco8 OLD nuclease |
-Macromolecule #3: RNA (83-MER)
| Macromolecule | Name: RNA (83-MER) / type: rna / ID: 3 / Number of copies: 4 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 26.660795 KDa |
| Sequence | String: AGAAGCUUCU UCUUCGAUAG AAGCUGAGGA GUCCAGUUUG ACUGGAUAAG GUGUUCGCCA UCUCUAGCCU CAGUAAAAAC UAG GENBANK: GENBANK: CP057441.1 |
-Macromolecule #4: DNA (75-MER)
| Macromolecule | Name: DNA (75-MER) / type: dna / ID: 4 / Number of copies: 4 / Classification: DNA |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 23.126848 KDa |
| Sequence | String: (DC)(DA)(DA)(DG)(DA)(DC)(DC)(DA)(DA)(DT) (DC)(DT)(DT)(DT)(DA)(DC)(DA)(DC)(DT)(DC) (DT)(DG)(DT)(DG)(DA)(DG)(DT)(DA)(DT) (DT)(DA)(DA)(DA)(DG)(DT)(DT)(DA)(DC)(DC) (DT) (DA)(DT)(DA)(DG)(DC)(DG) ...String: (DC)(DA)(DA)(DG)(DA)(DC)(DC)(DA)(DA)(DT) (DC)(DT)(DT)(DT)(DA)(DC)(DA)(DC)(DT)(DC) (DT)(DG)(DT)(DG)(DA)(DG)(DT)(DA)(DT) (DT)(DA)(DA)(DA)(DG)(DT)(DT)(DA)(DC)(DC) (DT) (DA)(DT)(DA)(DG)(DC)(DG)(DC)(DC) (DA)(DA)(DG)(DT)(DG)(DC)(DG)(DC)(DA)(DA) (DA)(DG) (DG)(DA)(DT)(DG)(DA)(DG)(DC) (DT)(DA)(DG)(DT)(DT)(DT)(DT)(DT) GENBANK: GENBANK: CP057441.1 |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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FIELD EMISSION GUN
