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	The bacteriophage ϕ29 tail possesses a pore-forming loop for cell membrane penetration.
Journal, issue, pages	Nature, Vol. 534, Issue 7608, Page 544-547, Year 2016
Publish date	Jun 23, 2016
Authors	Jingwei Xu / Miao Gui / Dianhong Wang / Ye Xiang /
PubMed Abstract	Most bacteriophages are tailed bacteriophages with an isometric or a prolate head attached to a long contractile, long non-contractile, or short non-contractile tail. The tail is a complex machine ...Most bacteriophages are tailed bacteriophages with an isometric or a prolate head attached to a long contractile, long non-contractile, or short non-contractile tail. The tail is a complex machine that plays a central role in host cell recognition and attachment, cell wall and membrane penetration, and viral genome ejection. The mechanisms involved in the penetration of the inner host cell membrane by bacteriophage tails are not well understood. Here we describe structural and functional studies of the bacteriophage ϕ29 tail knob protein gene product 9 (gp9). The 2.0 Å crystal structure of gp9 shows that six gp9 molecules form a hexameric tube structure with six flexible hydrophobic loops blocking one end of the tube before DNA ejection. Sequence and structural analyses suggest that the loops in the tube could be membrane active. Further biochemical assays and electron microscopy structural analyses show that the six hydrophobic loops in the tube exit upon DNA ejection and form a channel that spans the lipid bilayer of the membrane and allows the release of the bacteriophage genomic DNA, suggesting that cell membrane penetration involves a pore-forming mechanism similar to that of certain non-enveloped eukaryotic viruses. A search of other phage tail proteins identified similar hydrophobic loops, which indicates that a common mechanism might be used for membrane penetration by prokaryotic viruses. These findings suggest that although prokaryotic and eukaryotic viruses use apparently very different mechanisms for infection, they have evolved similar mechanisms for breaching the cell membrane.
External links	Nature / PubMed:27309813
Methods	EM (single particle) / X-ray diffraction
Resolution	2.039 - 34.5 Å
Structure data	EMDB-6556: Cryo-EM of bacteriophage phi29 emptied particles treated by low pH CsCl-gradient-purified Method: EM (single particle) / Resolution: 10.1 Å EMDB-6557: Cryo-EM of bacteriophage phi29 emptied particles treated by low pH without CsCl-gradient-purify Method: EM (single particle) / Resolution: 15.0 Å EMDB-6558: Cryo-EM of bacteriophage phi29 emptied particles fusing with liposome after low pH treatment Method: EM (single particle) / Resolution: 34.5 Å PDB-5fb4: Crystal structure of the bacteriophage phi29 tail knob protein gp9 truncation variant Method: X-RAY DIFFRACTION / Resolution: 2.039 Å PDB-5fb5: Crystal structure of the bacteriophage phi29 tail knob protein gp9 Method: X-RAY DIFFRACTION / Resolution: 3.5 Å PDB-5fei: Crystal structure of the bacteriophage phi29 tail knob protein gp9 truncation variant Method: X-RAY DIFFRACTION / Resolution: 2.604 Å
Chemicals	ChemComp-PEG: DI(HYDROXYETHYL)ETHER ChemComp-HOH: WATER
Source	bacillus phage phi29 (virus)
Keywords	VIRAL PROTEIN / bacteriophage phi29 / tail knob / tail knob protein gp9 / full-length