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Open data
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Basic information
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| Title | cryo-EM structure of retron Eco2 | |||||||||
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Keywords | RNA-mediated retron Eco2 oligomerization / RNA BINDING PROTEIN/DNA/RNA / RNA BINDING PROTEIN-DNA-RNA complex | |||||||||
| Function / homology | Function and homology informationribonuclease H / RNA-directed DNA polymerase / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / defense response to virus / RNA binding / metal ion binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||
Authors | Wang YJ / Wang C / Guan ZY / Zou TT | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Cell Discov / Year: 2025Title: Structural basis of the RNA-mediated Retron-Eco2 oligomerization. Authors: Yanjing Wang / Chen Wang / Yongqi Yin / Yongqing Cui / Zhikang Dai / Chang Liu / Yanke Chen / Zeyuan Guan / Tingting Zou / ![]() Abstract: In the evolutionary arms race between bacteria and viruses, retrons have emerged as distinctive antiphage defense systems. Here, we elucidate the structure and function of Retron-Eco2, which ...In the evolutionary arms race between bacteria and viruses, retrons have emerged as distinctive antiphage defense systems. Here, we elucidate the structure and function of Retron-Eco2, which comprises a non-coding RNA (ncRNA) that encodes multicopy single-stranded DNA (msDNA, a DNA‒RNA hybrid) and a fusion protein containing a reverse transcriptase (RT) domain and a topoisomerase-primase-like (Toprim) effector domain. The Eco2 msDNA and RT-Toprim fusion protein form a 1:1 stoichiometric nucleoprotein complex that further assembles into a trimer (msDNA:RT-Toprim ratio of 3:3) with a distinctive triangular configuration. The RNA portion of the msDNA in one protomer closely intertwines around the RT domain of an adjacent protomer, mediating the formation of this self-inhibitory assembly. Upon activation, the Toprim effector domain exhibits RNase activity, degrading RNA to arrest phage replication. We further reveal that phage mutants evading Eco2-mediated defense harbor mutations in the endonuclease IV-like protein DenB, underscoring DenB's critical role in triggering the activation of this system. Together, these findings provide key structural and functional insights into Retron-Eco2, laying the groundwork for harnessing its potential in biotechnology and synthetic biology applications. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_63214.map.gz | 49.7 MB | EMDB map data format | |
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| Header (meta data) | emd-63214-v30.xml emd-63214.xml | 17.7 KB 17.7 KB | Display Display | EMDB header |
| Images | emd_63214.png | 107 KB | ||
| Filedesc metadata | emd-63214.cif.gz | 6.1 KB | ||
| Others | emd_63214_half_map_1.map.gz emd_63214_half_map_2.map.gz | 49 MB 49 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-63214 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-63214 | HTTPS FTP |
-Validation report
| Summary document | emd_63214_validation.pdf.gz | 813.1 KB | Display | EMDB validaton report |
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| Full document | emd_63214_full_validation.pdf.gz | 812.7 KB | Display | |
| Data in XML | emd_63214_validation.xml.gz | 12 KB | Display | |
| Data in CIF | emd_63214_validation.cif.gz | 14.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-63214 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-63214 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9lm3MC 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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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_63214.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_63214_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_63214_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : retron Eco2
| Entire | Name: retron Eco2 |
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| Components |
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-Supramolecule #1: retron Eco2
| Supramolecule | Name: retron Eco2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Retron Ec67 protein
| Macromolecule | Name: Retron Ec67 protein / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO / EC number: RNA-directed DNA polymerase |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 68.673102 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MTKTSKLDAL RAATSREDLA KILDVKLVFL TNVLYRIGSD NQYTQFTIPK KGKGVRTISA PTDRLKDIQR RICDLLSDCR DEIFAIRKI SNNYSFGFER GKSIILNAYK HRGKQIILNI DLKDFFESFN FGRVRGYFLS NQDFLLNPVV ATTLAKAACY N GTLPQGSP ...String: MTKTSKLDAL RAATSREDLA KILDVKLVFL TNVLYRIGSD NQYTQFTIPK KGKGVRTISA PTDRLKDIQR RICDLLSDCR DEIFAIRKI SNNYSFGFER GKSIILNAYK HRGKQIILNI DLKDFFESFN FGRVRGYFLS NQDFLLNPVV ATTLAKAACY N GTLPQGSP CSPIISNLIC NIMDMRLAKL AKKYGCTYSR YADDITISTN KNTFPLEMAT VQPEGVVLGK VLVKEIENSG FE INDSKTR LTYKTSRQEV TGLTVNRIVN IDRCYYKKTR ALAHALYRTG EYKVPDENGV LVSGGLDKLE GMFGFIDQVD KFN NIKKKL NKQPDRYVLT NATLHGFKLK LNAREKAYSK FIYYKFFHGN TCPTIITEGK TDRIYLKAAL HSLETSYPEL FREK TDSKK KEINLNIFKS NEKTKYFLDL SGGTADLKKF VERYKNNYAS YYGSVPKQPV IMVLDNDTGP SDLLNFLRNK VKSCP DDVT EMRKMKYIHV FYNLYIVLTP LSPSGEQTSM EDLFPKDILD IKIDGKKFNK NNDGDSKTEY GKHIFSMRVV RDKKRK IDF KAFCCIFDAI KDIKEHYKLM LNSLEHHHHH HHH UniProtKB: Retron Ec67 protein |
-Macromolecule #2: DNA (67-MER)
| Macromolecule | Name: DNA (67-MER) / type: dna / ID: 2 Details: the correct sequence is: TCCTTCGCACAGCACACCTGCCGTATAGCTCTGAATCAAGGATTTTAGGGAGGCGATTCCTCCTGCC. Number of copies: 3 / Classification: DNA |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 20.522113 KDa |
| Sequence | String: (DT)(DC)(DC)(DT)(DT)(DC)(DG)(DC)(DA)(DC) (DA)(DG)(DC)(DA)(DC)(DA)(DC)(DC)(DT)(DG) (DC)(DC)(DG)(DT)(DA)(DT)(DA)(DG)(DC) (DT)(DC)(DT)(DG)(DA)(DA)(DT)(DC)(DA)(DA) (DG) (DG)(DA)(DT)(DT)(DT)(DT) ...String: (DT)(DC)(DC)(DT)(DT)(DC)(DG)(DC)(DA)(DC) (DA)(DG)(DC)(DA)(DC)(DA)(DC)(DC)(DT)(DG) (DC)(DC)(DG)(DT)(DA)(DT)(DA)(DG)(DC) (DT)(DC)(DT)(DG)(DA)(DA)(DT)(DC)(DA)(DA) (DG) (DG)(DA)(DT)(DT)(DT)(DT)(DA)(DG) (DG)(DG)(DA)(DG)(DG)(DC)(DG)(DA)(DT)(DT) (DC)(DC) (DT)(DC)(DC)(DT)(DG)(DC)(DC) |
-Macromolecule #5: DNA (5'-D(P*GP*GP*A)-3')
| Macromolecule | Name: DNA (5'-D(P*GP*GP*A)-3') / type: dna / ID: 5 / Number of copies: 3 / Classification: DNA |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 926.661 Da |
| Sequence | String: (DG)(DG)(DA) |
-Macromolecule #3: RNA (62-MER)
| Macromolecule | Name: RNA (62-MER) / type: rna / ID: 3 / Number of copies: 3 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 20.075932 KDa |
| Sequence | String: CACGCAUGUA GGCAGAUUUG UUGGUUGUGA AUCGCAACCA GUGGCCUUAA UGGCAGGAGG AA GENBANK: GENBANK: M55249.1 |
-Macromolecule #4: RNA (5'-R(*GP*UP*GP*CP*CP*UP*GP*CP*AP*UP*GP*CP*GP*U)-3')
| Macromolecule | Name: RNA (5'-R(*GP*UP*GP*CP*CP*UP*GP*CP*AP*UP*GP*CP*GP*U)-3') type: rna / ID: 4 / Number of copies: 3 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 4.455668 KDa |
| Sequence | String: GUGCCUGCAU GCGU |
-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: GATAN K3 BIOQUANTUM (6k 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: 1.8 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
China, 1 items
Citation


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Processing
FIELD EMISSION GUN
