11OK
Phage Tail Tube Protein from ALys extract
Summary for 11OK
| Entry DOI | 10.2210/pdb11ok/pdb |
| EMDB information | 72138 |
| Descriptor | Phage tail tube protein (1 entity in total) |
| Functional Keywords | helical assembly, phage tail tube protein, viral protein |
| Biological source | Bacteriophage sp. (unidentified bacteriophage) |
| Total number of polymer chains | 12 |
| Total formula weight | 207341.02 |
| Authors | Schaefer, J.H.,Lander, G.C. (deposition date: 2026-03-06, release date: 2026-07-01, Last modification date: 2026-07-15) |
| Primary citation | Schafer, J.H.,O'Neill, R.T.,Grotjahn, D.,Powers, E.T.,Kelly, J.W.,Lander, G.C. Siphoviridae phage tails co-enrich with ex vivo amyloids. Biorxiv, 2026 Cited by PubMed Abstract: Bacteriophages are ubiquitous in the environment and are part of the natural human microbiome. Despite their abundance, the role of the human phagome in health and disease remains poorly understood. Here, we identify phage tails in ex vivo amyloid extracts from patients with lysozyme amyloidosis (ALys) and light-chain amyloidosis (AL). Using cryo-EM analysis of the ALys dataset, automated model building, and database searches, we assigned the observed tubular assemblies to a phage tail tube protein (TTP). Although we cannot fully rule out the possibility of contamination, the presence of phage tails raises the question of whether they bind to and are co-purified with amyloid fibrils. These structures may provide further insight into the potential relationship between phage-derived assemblies and amyloid remodeling, with possible implications for future therapeutic strategies in human amyloidosis. PubMed: 42367858DOI: 10.64898/2026.06.17.733002 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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