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8I4M

Portal-tail complex structure of the Cyanophage P-SCSP1u

This is a non-PDB format compatible entry.
Summary for 8I4M
Entry DOI10.2210/pdb8i4m/pdb
EMDB information35175
DescriptorPortal protein(gp 16) of the cyanophage P-SCSP1u, Nozzle protein(gp 23) of the cyanophage P-SCSP1u, Adaptor protein(gp22) of the cyanophage P-SCSP1u, ... (4 entities in total)
Functional Keywordswhole virus, capsid, cyanophage, t7-like virus, virus
Biological sourceProchlorococcus phage P-SCSP1u
More
Total number of polymer chains48
Total formula weight3597351.19
Authors
Liu, H.,Dang, S. (deposition date: 2023-01-19, release date: 2023-11-01, Last modification date: 2024-05-08)
Primary citationCai, L.,Liu, H.,Zhang, W.,Xiao, S.,Zeng, Q.,Dang, S.
Cryo-EM structure of cyanophage P-SCSP1u offers insights into DNA gating and evolution of T7-like viruses.
Nat Commun, 14:6438-6438, 2023
Cited by
PubMed Abstract: Cyanophages, together with their host cyanobacteria, play important roles in marine biogeochemical cycles and control of marine food webs. The recently identified MPP-C (Marine Picocyanobacteria Podovirus clade C) cyanophages, belonging to the T7-like podoviruses, contain the smallest genomes among cyanopodoviruses and exhibit distinct infection kinetics. However, understanding of the MPP-C cyanophage infection process is hindered by the lack of high-resolution structural information. Here, we report the cryo-EM structure of the cyanophage P-SCSP1u, a representative member of the MPP-C phages, in its native form at near-atomic resolution, which reveals the assembly mechanism of the capsid and molecular interaction of the portal-tail complex. Structural comparison of the capsid proteins of P-SCSP1u and other podoviruses with known structures provides insights into the evolution of T7-like viruses. Furthermore, our study provides the near-atomic resolution structure of portal-tail complex for T7-like viruses. On the basis of previously reported structures of phage T7, we identify an additional valve and gate to explain the DNA gating mechanism for the T7-like viruses.
PubMed: 37833330
DOI: 10.1038/s41467-023-42258-7
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.81 Å)
Structure validation

227344

數據於2024-11-13公開中

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