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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Cryo-EM hexamer map of the elongating EcDRT3 complex | |||||||||
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Sample |
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Keywords | DRT3-ncRNA complex / reverse transcriptase / Anti-phage complex / IMMUNE SYSTEM | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||
Authors | Deng P / Gao A | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Science / Year: 2026Title: Protein-templated synthesis of dinucleotide repeat DNA by an antiphage reverse transcriptase. Authors: Pujuan Deng / Hyunbin Lee / Carlo Armijo / Haoqing Wang / Alex Gao / ![]() Abstract: Defense-associated reverse transcriptases (DRTs) are widespread bacterial anti-phage systems that use unconventional mechanisms of polynucleotide synthesis. We show that DRT3, which comprises two ...Defense-associated reverse transcriptases (DRTs) are widespread bacterial anti-phage systems that use unconventional mechanisms of polynucleotide synthesis. We show that DRT3, which comprises two distinct RTs (Drt3a and Drt3b) and a noncoding RNA (ncRNA), synthesizes alternating poly(GT/AC) double-stranded DNA. Cryo-electron microscopy structures at 2.6 Å resolution reveal a D3-symmetric 6:6:6 complex of Drt3a, Drt3b, and ncRNA. Drt3a produces the poly(GT) strand using a conserved ACACAC template within the ncRNA. Notably, Drt3b synthesizes a complementary, protein-primed poly(AC) strand in the complete absence of a nucleic acid template, using conserved active site residues specific to Drt3b to enforce precise base alternation. These findings expand the functional landscape of nucleic acid polymerases, revealing a protein-templated mechanism for sequence-specific DNA synthesis. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_73864.map.gz | 20.8 MB | EMDB map data format | |
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| Header (meta data) | emd-73864-v30.xml emd-73864.xml | 22.8 KB 22.8 KB | Display Display | EMDB header |
| Images | emd_73864.png | 83.7 KB | ||
| Filedesc metadata | emd-73864.cif.gz | 7 KB | ||
| Others | emd_73864_half_map_1.map.gz emd_73864_half_map_2.map.gz | 621.2 MB 621.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-73864 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-73864 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_73864.map.gz / Format: CCP4 / Size: 669.9 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: 0.8409 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_73864_half_map_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Half map: #1
| File | emd_73864_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Hexameric complex of DRT3-ncRNA
| Entire | Name: Hexameric complex of DRT3-ncRNA |
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| Components |
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-Supramolecule #1: Hexameric complex of DRT3-ncRNA
| Supramolecule | Name: Hexameric complex of DRT3-ncRNA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Drt3a reverse transcriptase protein
| Macromolecule | Name: Drt3a reverse transcriptase protein / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 50.34575 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MYDQSFNPRT LSRCFKPEDF QKNRALSLDS VREKTIRAAI ERFNNGFLGY NLRSSVLRGK KVYWADELAD TLVLRKVQSN LSNLYQLKL PSRTMIVDTL NVFLSECSQY KLYRLDIHSF YESFNKDYIF KKIDELERLE MKTKQLLKEF LYSFYLTGGE G IPRGLSIS ...String: MYDQSFNPRT LSRCFKPEDF QKNRALSLDS VREKTIRAAI ERFNNGFLGY NLRSSVLRGK KVYWADELAD TLVLRKVQSN LSNLYQLKL PSRTMIVDTL NVFLSECSQY KLYRLDIHSF YESFNKDYIF KKIDELERLE MKTKQLLKEF LYSFYLTGGE G IPRGLSIS AYLAELLMHD FDNHLKDDKS VFYYARYVDD IVIVTSGFED SNAFIENVKS ILPPGLSFNE GEKYYISDLI PK SANKKNT HHHHHHESPT KLLTFEYLGY DFSVGDKIEE CNIRGFYRLI EVDLAHAKAN KIKSRIIYSI IDYNKTKDFE LLC ERLKFL STNFSILDSG RVLKRLSGIH YNYPLVDART SRRLAELDLF LRKAVLSSNG KVFFDFHANL NQYKKYRLLK ISFV RGHEK RHFFHYSASK MMRIQRCWKY V |
-Macromolecule #2: Drt3b reverse transcriptase protein
| Macromolecule | Name: Drt3b reverse transcriptase protein / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 76.426602 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSKKKEVRVN KKDFNRVLVT ETIPYETPII VSNDGFYNNV VKHQTANDIA KLLTQRVILG ERKKGRYTIP YVFKINKNET EFRRLAFPH PISQIEMRDF YLHFNQVMIN FCSKSDFSIR RPVKVASTYY YKNLLEDKNL YKRGPVDTDK NELLTRHASS Y FGYHGYDR ...String: MSKKKEVRVN KKDFNRVLVT ETIPYETPII VSNDGFYNNV VKHQTANDIA KLLTQRVILG ERKKGRYTIP YVFKINKNET EFRRLAFPH PISQIEMRDF YLHFNQVMIN FCSKSDFSIR RPVKVASTYY YKNLLEDKNL YKRGPVDTDK NELLTRHASS Y FGYHGYDR LYKFFMSNDF IDLERKYNTL YTLDVSKCFD SIYTHSISWA TKTKTFTKGM LANKSLNFGD AFDKLMQRCN FN ETHGVII GPEISRIFAE IIFQKIDLNV QFKLRNIDTP LNKGVDYDIR RYVDDVFIFS KNEVNAEIIY KVYADKLNEY NMH VNLGKV TKNSRPFITA KTQIIHHVNQ KMNVFIDSFL SYDDEMKLIA KPIYNNRKLA NKFIDEVKII CSERKSGYGE VSSY IVSAI FERIKRLTSS VNQAEDKDIY NVMYVLLHIS LFFFRVAPSV SSSYKLASIL IVTLRYFKAQ VPSYSDLIAS YIYFE IEDF LKAAKNGKKT IDNLVSLEAY NIMYVIGELD QDRYLSKQLV EDVFSEVDSY FDIVSCLYIV KDKKVYDSLK NNIIDV INS KLMSSDNILD YSEKAMLFLD VMSCPYIDLK WKKIWLKSIL KELQEATPNN NEIDSFISYS VANPWFVDWS NVDLLNF LE KKQLKKA(PTR) |
-Macromolecule #3: non-coding RNA
| Macromolecule | Name: non-coding RNA / type: rna / ID: 3 / Number of copies: 6 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 44.236227 KDa |
| Sequence | String: AAUGCAACCA AUAUGCCCUA CACGAUUUUU CGAUAUACUA GGGCUGAUUA CGGUAGGUAA GUUACACGUA ACCUUAGCUA CCUUAUGAC GCUCAAGAGC AGCAAUGCAC ACACUAAGGG AUGAGGUUGC UUCAAUUUC GENBANK: GENBANK: CP053259.1 |
-Macromolecule #4: cDNA (5'-D(P*TP*GP*TP*GP*TP*GP*TP*GP*TP*GP*TP*GP*TP*GP*TP*GP*T)-3')
| Macromolecule | Name: cDNA (5'-D(P*TP*GP*TP*GP*TP*GP*TP*GP*TP*GP*TP*GP*TP*GP*TP*GP*T)-3') type: dna / ID: 4 / Number of copies: 6 / Classification: DNA |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 5.326424 KDa |
| Sequence | String: (DT)(DG)(DT)(DG)(DT)(DG)(DT)(DG)(DT)(DG) (DT)(DG)(DT)(DG)(DT)(DG)(DT) |
-Macromolecule #5: cDNA (5'-D(P*CP*AP*CP*AP*CP*AP*CP*AP*CP*AP*CP*AP*CP*AP*CP*AP*CP*A)-3')
| Macromolecule | Name: cDNA (5'-D(P*CP*AP*CP*AP*CP*AP*CP*AP*CP*AP*CP*AP*CP*AP*CP*AP*CP*A)-3') type: dna / ID: 5 / Number of copies: 6 / Classification: DNA |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 5.37654 KDa |
| Sequence | String: (DC)(DA)(DC)(DA)(DC)(DA)(DC)(DA)(DC)(DA) (DC)(DA)(DC)(DA)(DC)(DA)(DC)(DA) |
-Macromolecule #6: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 6 / Number of copies: 18 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #7: PYROPHOSPHATE 2-
| Macromolecule | Name: PYROPHOSPHATE 2- / type: ligand / ID: 7 / Number of copies: 6 / Formula: POP |
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| Molecular weight | Theoretical: 175.959 Da |
| Chemical component information | ![]() ChemComp-POP: |
-Macromolecule #8: water
| Macromolecule | Name: water / type: ligand / ID: 8 / Number of copies: 6 / Formula: HOH |
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| Molecular weight | Theoretical: 18.015 Da |
| Chemical component information | ![]() ChemComp-HOH: |
-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: 7.5 |
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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 (6k x 4k) / Average electron dose: 40.0 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: 2.0 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model / Details: ModelAngelo |
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| Refinement | Space: REAL / Protocol: AB INITIO MODEL |
| Output model | ![]() PDB-9z6y: |
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About Yorodumi




Keywords
Authors
United States, 1 items
Citation











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FIELD EMISSION GUN
