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8HO3

Capsid of DT57C bacteriophage in the full state

Summary for 8HO3
Entry DOI10.2210/pdb8ho3/pdb
EMDB information34920
DescriptorMajor head protein (1 entity in total)
Functional Keywordscapsid, t5, mhp, virus
Biological sourceEscherichia phage DT57C
Total number of polymer chains13
Total formula weight658988.17
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: 2022-12-09, release date: 2023-12-13, Last modification date: 2023-12-27)
Primary citationAyala, 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: 38081816
DOI: 10.1038/s41467-023-43824-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

227111

數據於2024-11-06公開中

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