23SH
The composite Cryo-EM structure of the tail region of bacteriophage RAN69
Summary for 23SH
| Entry DOI | 10.2210/pdb23sh/pdb |
| EMDB information | 69212 |
| Descriptor | tail spike gp1, nozzle gp13, tail fiber gp9, ... (5 entities in total) |
| Functional Keywords | bacteriophage, ran69, tail, virus |
| Biological source | Klebsiella phage RAN69 More |
| Total number of polymer chains | 11 |
| Total formula weight | 526875.03 |
| Authors | |
| Primary citation | Ruan, Z.,Hu, H.,Wang, A.,Shao, Q.,Li, X.,Xie, L.,Sun, Z.,Yu, J.,Fang, Q. Near-complete cryo-EM structure of the Klebsiella pneumoniae podophage RAN69 reveals tail fiber-spike interface and a divergent pre-ejectosome. Structure, 2026 Cited by PubMed Abstract: Carbapenem-resistant Klebsiella pneumoniae is a critical-priority pathogen, underscoring the need for alternatives to antibiotics. Bacteriophages are promising agents, yet high-resolution structures of K. pneumoniae phages are scarce. Here, we report near-complete cryo-electron microscopic reconstructions of the K. pneumoniae podophage RAN69 at 3.0-3.4 Å resolution, enabling atomic models for 12 structural components. Complete in situ structures of the long tail fiber (gp9 trimer) and distal tail spike (gp1 trimer) are resolved, revealing a previously unknown binding interface in which the gp1 N-terminal arm wedges between spike-binding domains of gp9. The pre-ejectosome forms a conserved double-layered assembly (gp10 tetramer over gp11 octamer), tethered to the portal by an octameric gp12 that inserts long helices into the portal barrel, with gp20 reinforcing gp11 interfaces. Divergent folds in gp10 and a lysozyme-like gp11 peripheral domain suggest adaptation to host envelopes. These structures advance our understanding of podophage assembly. PubMed: 42314677DOI: 10.1016/j.str.2026.05.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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