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	Structural changes in bacteriophage T7 upon receptor-induced genome ejection.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 118, Issue 37, Year 2021
Publish date	Sep 14, 2021
Authors	Wenyuan Chen / Hao Xiao / Li Wang / Xurong Wang / Zhixue Tan / Zhen Han / Xiaowu Li / Fan Yang / Zhonghua Liu / Jingdong Song / Hongrong Liu / Lingpeng Cheng /
PubMed Abstract	Many tailed bacteriophages assemble ejection proteins and a portal-tail complex at a unique vertex of the capsid. The ejection proteins form a transenvelope channel extending the portal-tail channel ...Many tailed bacteriophages assemble ejection proteins and a portal-tail complex at a unique vertex of the capsid. The ejection proteins form a transenvelope channel extending the portal-tail channel for the delivery of genomic DNA in cell infection. Here, we report the structure of the mature bacteriophage T7, including the ejection proteins, as well as the structures of the full and empty T7 particles in complex with their cell receptor lipopolysaccharide. Our near-atomic-resolution reconstruction shows that the ejection proteins in the mature T7 assemble into a core, which comprises a fourfold gene product 16 (gp16) ring, an eightfold gp15 ring, and a putative eightfold gp14 ring. The gp15 and gp16 are mainly composed of helix bundles, and gp16 harbors a lytic transglycosylase domain for degrading the bacterial peptidoglycan layer. When interacting with the lipopolysaccharide, the T7 tail nozzle opens. Six copies of gp14 anchor to the tail nozzle, extending the nozzle across the lipopolysaccharide lipid bilayer. The structures of gp15 and gp16 in the mature T7 suggest that they should undergo remarkable conformational changes to form the transenvelope channel. Hydrophobic α-helices were observed in gp16 but not in gp15, suggesting that gp15 forms the channel in the hydrophilic periplasm and gp16 forms the channel in the cytoplasmic membrane.
External links	Proc Natl Acad Sci U S A / PubMed:34504014 / PubMed Central
Methods	EM (single particle)
Resolution	3.4 - 15.1 Å
Structure data	EMDB-31315: Symmety-mismatch Reconstruction of Mature T7 Method: EM (single particle) / Resolution: 7.0 Å EMDB-31316: core-portal-tail complex Method: EM (single particle) / Resolution: 5.8 Å 31317 7eyb EMDB-31317: core proteins of mature t7 PDB-7eyb: core proteins Method: EM (single particle) / Resolution: 3.7 Å EMDB-31318: LPS-treated empty bacteriophage T7 Method: EM (single particle) / Resolution: 8.2 Å 31319 7ey8 7ey9 EMDB-31319: portal-tail complex of mature T7 PDB-7ey8: portal PDB-7ey9: tail proteins Method: EM (single particle) / Resolution: 3.4 Å EMDB-31320: LPS-treated full bacteriophage T7 Method: EM (single particle) / Resolution: 15.1 Å 31321 7ey6 7ey7 EMDB-31321: Structural changes in bacteriophage T7 upon receptor-induced genome ejection PDB-7ey6: The portal protein (GP8) of bacteriophage T7 PDB-7ey7: bacteriophage T7 tail complex Method: EM (single particle) / Resolution: 4.3 Å EMDB-31322: portal-tail complex of LPS-treated full bacteriophage T7 Method: EM (single particle) / Resolution: 10.2 Å
Source	escherichia phage t7 (virus)
Keywords	VIRAL PROTEIN / bacteriophage T7 / VIRUS / bacteriophae T7 portal / bacteriophae T7 tail proteins / bacteriophage T7 core proteins