9Z6Z
Structure of the resting EcDRT3 reverse transcriptase in complex with its non-coding RNA
Summary for 9Z6Z
| Entry DOI | 10.2210/pdb9z6z/pdb |
| EMDB information | 73865 76002 |
| Descriptor | Drt3a reverse transcriptase protein, Drt3b reverse transcriptase protein, non-coding RNA, ... (7 entities in total) |
| Functional Keywords | drt3-ncrna complex, reverse transcriptase, anti-phage complex, immune system |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 30 |
| Total formula weight | 1079103.98 |
| Authors | |
| Primary citation | Deng, P.,Lee, H.,Armijo, C.,Wang, H.,Gao, A. Protein-templated synthesis of dinucleotide repeat DNA by an antiphage reverse transcriptase. Science, :eaed1656-eaed1656, 2026 Cited by PubMed 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 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. PubMed: 41990131DOI: 10.1126/science.aed1656 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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