9UFN
Phage T4 tip of the tail tube in post-tail-contraction state (genome-full particle)
Summary for 9UFN
| Entry DOI | 10.2210/pdb9ufn/pdb |
| EMDB information | 64113 |
| Descriptor | Tail tube protein gp19, Baseplate tail-tube junction protein gp54, Baseplate tail-tube junction protein gp48 (3 entities in total) |
| Functional Keywords | bacteriophage, myovirus, phage t4, tail contraction, phage hub complex, tape-measure protein, genome release, viral protein |
| Biological source | Escherichia phage T4 More |
| Total number of polymer chains | 4 |
| Total formula weight | 111744.79 |
| Authors | |
| Primary citation | Shao, Q.,Dong, J.,Wang, A.,Hu, H.,Yue, J.,Li, H.,Li, Y.,Zhang, Q.,Liu, J.,Sun, L.,Fokine, A.,Rao, V.B.,Tao, P.,Fang, Q. Cryo-EM Structures of Phage T4 Infection Intermediate. J.Mol.Biol., 438:169938-169938, 2026 Cited by PubMed Abstract: Myophage is endowed with a sophisticated contractile tail and infection machinery. However, the mechanisms of host recognition, signal transduction, and genome delivery remain poorly understood. Here, we capture a pre-genome-release intermediate of myophage T4 and determine its structure by cryo-electron microscopy. Comparative analysis of this tail-contracted, pre-genome-release intermediate structure with the mature T4 virion and the tail-contracted, post-genome-release structure reveals structural transitions in the tail, tape-measure protein (TMP), baseplate, and long tail fibers that drive genome delivery. Our findings further suggest that tail sheath contraction is coupled to a coordinated repositioning of the viral DNA-TMP complex, potentially facilitating genome translocation via charge-mediated interactions. It appears that the expelled TMP may further reorganize into a putative transmembrane complex that supports genome delivery into the host cytosol. PubMed: 42401366DOI: 10.1016/j.jmb.2026.169938 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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