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8GTC

Cryo-EM model of the marine siphophage vB_DshS-R4C baseplate-tail complex

This is a non-PDB format compatible entry.
Summary for 8GTC
Entry DOI10.2210/pdb8gtc/pdb
EMDB information34249
DescriptorMajor tail protein, Distal tail protein, Megatron protein, ... (5 entities in total)
Functional Keywordsmarine bacteriophage, cryo-em, siphophage, baseplate, megatron protein, tail fibre protein, distal tail protein, hub protein, viral protein
Biological sourceDinoroseobacter phage vB_DshS-R4C
More
Total number of polymer chains27
Total formula weight983646.39
Authors
Huang, Y.,Sun, H.,Wei, S.,Zheng, Q.,Li, S.,Zhang, R.,Xia, N. (deposition date: 2022-09-08, release date: 2023-07-12, Last modification date: 2024-06-19)
Primary citationHuang, Y.,Sun, H.,Wei, S.,Cai, L.,Liu, L.,Jiang, Y.,Xin, J.,Chen, Z.,Que, Y.,Kong, Z.,Li, T.,Yu, H.,Zhang, J.,Gu, Y.,Zheng, Q.,Li, S.,Zhang, R.,Xia, N.
Structure and proposed DNA delivery mechanism of a marine roseophage.
Nat Commun, 14:3609-3609, 2023
Cited by
PubMed Abstract: Tailed bacteriophages (order, Caudovirales) account for the majority of all phages. However, the long flexible tail of siphophages hinders comprehensive investigation of the mechanism of viral gene delivery. Here, we report the atomic capsid and in-situ structures of the tail machine of the marine siphophage, vB_DshS-R4C (R4C), which infects Roseobacter. The R4C virion, comprising 12 distinct structural protein components, has a unique five-fold vertex of the icosahedral capsid that allows genome delivery. The specific position and interaction pattern of the tail tube proteins determine the atypical long rigid tail of R4C, and further provide negative charge distribution within the tail tube. A ratchet mechanism assists in DNA transmission, which is initiated by an absorption device that structurally resembles the phage-like particle, RcGTA. Overall, these results provide in-depth knowledge into the intact structure and underlining DNA delivery mechanism for the ecologically important siphophages.
PubMed: 37330604
DOI: 10.1038/s41467-023-39220-y
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.5 Å)
Structure validation

237992

數據於2025-06-25公開中

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