PMID:26144253

Citation	Sun, L, Zhang, X, Gao, S, Rao, PA, Padilla-Sanchez, V, Chen, Z, Sun, S, Xiang, Y, Subramaniam, S, Rao, VB and Rossmann, MG (2015) Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution. Nat Commun 6:7548
Abstract	The structure and assembly of bacteriophage T4 has been extensively studied. However, the detailed structure of the portal protein remained unknown. Here we report the structure of the bacteriophage T4 portal assembly, gene product 20 (gp20), determined by cryo-electron microscopy (cryo-EM) to 3.6 Å resolution. In addition, analysis of a 10 Å resolution cryo-EM map of an empty prolate T4 head shows how the dodecameric portal assembly interacts with the capsid protein gp23 at the special pentameric vertex. The gp20 structure also verifies that the portal assembly is required for initiating head assembly, for attachment of the packaging motor, and for participation in DNA packaging. Comparison of the Myoviridae T4 portal structure with the known portal structures of φ29, SPP1 and P22, representing Podo- and Siphoviridae, shows that the portal structure probably dates back to a time when self-replicating microorganisms were being established on Earth.
Links	PubMed PMC4493910 Online version:10.1038/ncomms8548
Keywords	Bacteriophage T4/genetics; Bacteriophage T4/metabolism; Capsid Proteins/chemistry; Capsid Proteins/genetics; Capsid Proteins/metabolism; Cryoelectron Microscopy/methods; Gene Expression Regulation, Viral/physiology; Models, Molecular; Protein Conformation; Virus Assembly/physiology
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BPT4:PORTL		GO:0046798: viral portal complex	ECO:0000314:		C		This is a ring of proteins where DNA enters and exits the phages capsid. The structure was determined by cryo-electron microscopy (cryo-EM) Figure 1.	complete CACAO 12005

References

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