Summary for 8HQZ
| Entry DOI | 10.2210/pdb8hqz/pdb |
| EMDB information | 34920 34949 34952 34955 |
| Descriptor | Baseplate hub protein, Distal tail protein, Minor tail protein, ... (7 entities in total) |
| Functional Keywords | baseplate, t5, virus, viral protein |
| Biological source | Escherichia phage DT57C More |
| Total number of polymer chains | 13 |
| Total formula weight | 773020.44 |
| Authors | Ayala, R.,Moiseenko, A.V.,Chen, T.H.,Kulikov, E.E.,Golomidova, A.K.,Orekhov, P.S.,Street, M.A.,Sokolova, O.S.,Letarov, A.V.,Wolf, M. (deposition date: 2022-12-14, release date: 2023-12-13, Last modification date: 2024-10-23) |
| Primary citation | Ayala, R.,Moiseenko, A.V.,Chen, T.H.,Kulikov, E.E.,Golomidova, A.K.,Orekhov, P.S.,Street, M.A.,Sokolova, O.S.,Letarov, A.V.,Wolf, M. Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers. Nat Commun, 14:8205-8205, 2023 Cited by PubMed Abstract: The T5 family of viruses are tailed bacteriophages characterized by a long non-contractile tail. The bacteriophage DT57C is closely related to the paradigmal T5 phage, though it recognizes a different receptor (BtuB) and features highly divergent lateral tail fibers (LTF). Considerable portions of T5-like phages remain structurally uncharacterized. Here, we present the structure of DT57C determined by cryo-EM, and an atomic model of the virus, which was further explored using all-atom molecular dynamics simulations. The structure revealed a unique way of LTF attachment assisted by a dodecameric collar protein LtfC, and an unusual composition of the phage neck constructed of three protein rings. The tape measure protein (TMP) is organized within the tail tube in a three-stranded parallel α-helical coiled coil which makes direct contact with the genomic DNA. The presence of the C-terminal fragment of the TMP that remains within the tail tip suggests that the tail tip complex returns to its original state after DNA ejection. Our results provide a complete atomic structure of a T5-like phage, provide insights into the process of DNA ejection as well as a structural basis for the design of engineered phages and future mechanistic studies. PubMed: 38081816DOI: 10.1038/s41467-023-43824-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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