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- PDB-9x3q: Phage T4 inner baseplate in post-tail-contraction state (genome-f... -

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Basic information

Entry
Database: PDB / ID: 9x3q
TitlePhage T4 inner baseplate in post-tail-contraction state (genome-full particle)
Components
  • Baseplate wedge protein gp25
  • Baseplate wedge protein gp53
  • Baseplate wedge protein gp6
  • Baseplate wedge protein gp7
  • Tail tube protein gp19
KeywordsVIRAL PROTEIN / Bacteriophage / Myovirus / Phage T4 / tail contraction / phage neck complex
Function / homology
Function and homology information


symbiont genome ejection through host cell envelope, contractile tail mechanism / virus tail, tube / virus tail, baseplate / viral tail assembly / structural molecule activity / identical protein binding
Similarity search - Function
Baseplate wedge protein gp53, bacteriophage T4 / Base plate wedge protein 53 / Baseplate wedge protein gp7 / : / : / : / Baseplate wedge protein gp7, domain V / Baseplate wedge protein gp7, helical domain / Baseplate wedge protein gp7, domain VI / Baseplate wedge protein gp6 ...Baseplate wedge protein gp53, bacteriophage T4 / Base plate wedge protein 53 / Baseplate wedge protein gp7 / : / : / : / Baseplate wedge protein gp7, domain V / Baseplate wedge protein gp7, helical domain / Baseplate wedge protein gp7, domain VI / Baseplate wedge protein gp6 / : / : / : / : / : / Baseplate wedge protein gp6-like, helical domain / Baseplate structural protein gp6, C-terminal domain I / Baseplate structural protein gp6, C-terminal domain II / Baseplate wedge protein gp6, domain II / Baseplate structural protein gp6, C-terminal domain III / IraD/Gp25-like / Baseplate wedge protein gp25 / Bacteriophage T4, Gp19, tail tube / T4-like virus tail tube protein gp19 / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Baseplate wedge protein gp25 / Tail tube protein gp19 / Baseplate wedge protein gp53 / Baseplate wedge protein gp6 / Baseplate wedge protein gp7
Similarity search - Component
Biological speciesEscherichia phage T4 (virus)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsShao, Q. / Dong, J. / Wang, A. / Hu, H. / Yue, J. / Li, H. / Li, Y. / Zhang, Q. / Liu, J. / Sun, L. ...Shao, Q. / Dong, J. / Wang, A. / Hu, H. / Yue, J. / Li, H. / Li, Y. / Zhang, Q. / Liu, J. / Sun, L. / Fokine, A. / Rao, V.B. / Tao, P. / Fang, Q.
Funding support China, United States, 7items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32371285 China
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI175340 United States
National Institutes of Health/National Institute on Drug Abuse (NIH/NIDA)DP1DA060580 United States
National Science Foundation (NSF, United States)MCB-0923873 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM124378 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM110243 United States
National Institutes of Health/Office of the Director1S10OD023603-01A1 United States
CitationJournal: J Mol Biol / Year: 2026
Title: Cryo-EM Structures of Phage T4 Infection Intermediate.
Authors: Qianqian Shao / Junhua Dong / Aohan Wang / Hongli Hu / Jian Yue / Hongmei Li / Yinyin Li / Qinfen Zhang / Jun Liu / Lei Sun / Andrei Fokine / Venigalla B Rao / Pan Tao / Qianglin Fang /
Abstract: 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. ...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.
History
DepositionOct 9, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jul 22, 2026Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: Mask / Part number: 1 / Data content type: Mask / Provider: repository / Type: Initial release
Revision 1.0Jul 22, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Baseplate wedge protein gp6
B: Baseplate wedge protein gp6
C: Baseplate wedge protein gp7
D: Baseplate wedge protein gp25
E: Baseplate wedge protein gp53
F: Tail tube protein gp19
G: Tail tube protein gp19


Theoretical massNumber of molelcules
Total (without water)343,3837
Polymers343,3837
Non-polymers00
Water00
1
A: Baseplate wedge protein gp6
B: Baseplate wedge protein gp6
C: Baseplate wedge protein gp7
D: Baseplate wedge protein gp25
E: Baseplate wedge protein gp53
F: Tail tube protein gp19
G: Tail tube protein gp19
x 6


Theoretical massNumber of molelcules
Total (without water)2,060,29842
Polymers2,060,29842
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation5

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Components

#1: Protein Baseplate wedge protein gp6 / Gene product 6 / gp6


Mass: 74492.641 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia phage T4 (virus) / References: UniProt: P19060
#2: Protein Baseplate wedge protein gp7 / Gene product 7 / gp7


Mass: 119336.516 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia phage T4 (virus) / References: UniProt: P19061
#3: Protein Baseplate wedge protein gp25 / Outer wedge of baseplate protein / Protein Gp25


Mass: 15111.101 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia phage T4 (virus) / References: UniProt: P09425
#4: Protein Baseplate wedge protein gp53 / Gene product 53 / gp53


Mass: 22990.885 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia phage T4 (virus) / References: UniProt: P16011
#5: Protein Tail tube protein gp19 / Gene product 19 / gp19


Mass: 18479.613 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia phage T4 (virus) / References: UniProt: P13333
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Escherichia phage T4 / Type: VIRUS / Entity ID: all / Source: NATURAL
Source (natural)Organism: Escherichia phage T4 (virus)
Details of virusEmpty: NO / Enveloped: NO / Isolate: STRAIN / Type: VIRION
Natural hostOrganism: Escherichia coli
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid type: C-flat-1.2/1.3
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recording
IDImaging-IDAverage exposure time (sec.)Electron dose (e/Å2)Detector modeFilm or detector modelNum. of real images
11840SUPER-RESOLUTIONGATAN K2 SUMMIT (4k x 4k)2276
21859.6GATAN K3 (6k x 4k)5090
EM imaging opticsEnergyfilter name: GIF Bioquantum
Image scans
Movie frames/imageIDImage recording-IDEntry-ID
32119X3Q
229X3Q

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Processing

EM software
IDNameVersionCategory
1RELION3.1particle selection
2PHENIX1.19.2_4158:model refinement
13RELION3.13D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 116671
SymmetryPoint symmetry: C6 (6 fold cyclic)
3D reconstructionResolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 40108 / Symmetry type: POINT

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