9x3q

Phage T4 inner baseplate in post-tail-contraction state (genome-full particle)

Structural highlights

9x3q is a 7 chain structure with sequence from Escherichia phage T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BP06_BPT4 Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.^[1] ^[2]

Publication Abstract from PubMed

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.

Cryo-EM Structures of Phage T4 Infection Intermediate.,Shao Q, Dong J, Wang A, Hu H, Yue J, Li H, Li Y, Zhang Q, Liu J, Sun L, Fokine A, Rao VB, Tao P, Fang Q J Mol Biol. 2026 Jul 4;438(19):169938. doi: 10.1016/j.jmb.2026.169938. PMID:42401366^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Leiman PG, Chipman PR, Kostyuchenko VA, Mesyanzhinov VV, Rossmann MG. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell. 2004 Aug 20;118(4):419-29. PMID:15315755 doi:10.1016/j.cell.2004.07.022
↑ Leiman PG, Arisaka F, van Raaij MJ, Kostyuchenko VA, Aksyuk AA, Kanamaru S, Rossmann MG. Morphogenesis of the T4 tail and tail fibers. Virol J. 2010 Dec 3;7:355. doi: 10.1186/1743-422X-7-355. PMID:21129200 doi:10.1186/1743-422X-7-355
↑ Shao Q, Dong J, Wang A, Hu H, Yue J, Li H, Li Y, Zhang Q, Liu J, Sun L, Fokine A, Rao VB, Tao P, Fang Q. Cryo-EM Structures of Phage T4 Infection Intermediate. J Mol Biol. 2026 Jul 4;438(19):169938. PMID:42401366 doi:10.1016/j.jmb.2026.169938

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OCA

[1] Leiman PG, Chipman PR, Kostyuchenko VA, Mesyanzhinov VV, Rossmann MG. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell. 2004 Aug 20;118(4):419-29. PMID:15315755 doi:10.1016/j.cell.2004.07.022

[2] Leiman PG, Arisaka F, van Raaij MJ, Kostyuchenko VA, Aksyuk AA, Kanamaru S, Rossmann MG. Morphogenesis of the T4 tail and tail fibers. Virol J. 2010 Dec 3;7:355. doi: 10.1186/1743-422X-7-355. PMID:21129200 doi:10.1186/1743-422X-7-355

[3] Shao Q, Dong J, Wang A, Hu H, Yue J, Li H, Li Y, Zhang Q, Liu J, Sun L, Fokine A, Rao VB, Tao P, Fang Q. Cryo-EM Structures of Phage T4 Infection Intermediate. J Mol Biol. 2026 Jul 4;438(19):169938. PMID:42401366 doi:10.1016/j.jmb.2026.169938

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[2]

[3]

9x3q

Phage T4 inner baseplate in post-tail-contraction state (genome-full particle)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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