Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	In situ structures of the portal-neck-tail complex of bacteriophage T4 inform a viral genome positioning mechanism.
Journal, issue, pages	Nat Commun, Vol. 17, Issue 1, Year 2026
Publish date	Feb 20, 2026
Authors	Andrei Fokine / Jingen Zhu / Thomas Klose / Frank Vago / Charles-Adrien Arnaud / Zhiqing Wang / Baldeep Khare / Michael G Rossmann / Zhenguo Chen / Lei Sun / Qianglin Fang / Richard J Kuhn / Venigalla B Rao /
PubMed Abstract	The post-genome packaging mechanisms that govern the assembly of an infectious virion are poorly understood in bacteriophages and other viruses. Here, our near-atomic resolution cryo-EM structural ...The post-genome packaging mechanisms that govern the assembly of an infectious virion are poorly understood in bacteriophages and other viruses. Here, our near-atomic resolution cryo-EM structural analyses uncovered an assembly- and conformation-driven genome positioning mechanism in the tailed bacteriophage T4. We show that following headful packaging, which generates a pressurized head, a global conformational change occurs in the portal structure, probably triggering packaging termination and ejection of the packaging motor. Our high-resolution structures of the neck of the virion further show that the neck undergoes conformational changes upon docking of a pre-assembled tail onto the sealed neck, which then opens a genome-gate. Driven by the pressure of the packaged DNA, the genome travels through open neck channels, binds and compresses the resident tape-measure protein, and halts at the bottom of the second topmost disk of the tail tube. Pressure-suspended within the virion's innermost tunnel and secured by a baseplate plug, the genome remains poised to flow through the tunnel into a host cell upon receiving the host receptor recognition signal.
External links	Nat Commun / PubMed:41720772 / PubMed Central
Methods	EM (single particle)
Resolution	3.3 - 3.8 Å
Structure data	48324 9mkb EMDB-48324, PDB-9mkb: Structure of the bacteriophage T4 portal-neck-tail complex Method: EM (single particle) / Resolution: 3.8 Å 48458 9mof EMDB-48458, PDB-9mof: Structure of the bacteriophage T4 portal-neck-tail connector complex Method: EM (single particle) / Resolution: 3.8 Å 48459 9mog EMDB-48459, PDB-9mog: Structure of the distal part of the bacteriophage T4 tail Method: EM (single particle) / Resolution: 3.6 Å 48460 9moh EMDB-48460, PDB-9moh: Structure of the middle part of the bacteriophage T4 tail Method: EM (single particle) / Resolution: 3.4 Å EMDB-48462: 6-fold-symmetric reconstruction focused on the bacteriophage T4 neck region Method: EM (single particle) / Resolution: 3.3 Å EMDB-48463: 6-fold-symmetric reconstruction focused on the middle part of the bacteriophage T4 tail Method: EM (single particle) / Resolution: 3.3 Å EMDB-48464: 6-fold-symmetric reconstruction focused on the bacteriophage T4 baseplate Method: EM (single particle) / Resolution: 3.4 Å
Chemicals	ChemComp-ZN: Unknown entry
Source	escherichia phage t4 (virus)
Keywords	VIRAL PROTEIN / bacteriophage T4 / portal vertex / phage neck / phage tail / contractile sheath / tail tube / baseplate / VIRUS / tail terminator protein / tube terminator protein / asymmetric phage reconstruction / DNA retention / neck stopper protein / head completion proteins / contractile tail / contractile phage tail / sheath protein / tail tube protein