EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	The bacteriophage ϕ29 tail possesses a pore-forming loop for cell membrane penetration.
ジャーナル・号・ページ	Nature, Vol. 534, Issue 7608, Page 544-547, Year 2016
掲載日	2016年6月23日
著者	Jingwei Xu / Miao Gui / Dianhong Wang / Ye Xiang /
PubMed 要旨	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.
リンク	Nature / PubMed:27309813
手法	EM (単粒子) / X線回折
解像度	2.039 - 34.5 Å
構造データ	EMDB-6556: Cryo-EM of bacteriophage phi29 emptied particles treated by low pH CsCl-gradient-purified 手法: EM (単粒子) / 解像度: 10.1 Å EMDB-6557: Cryo-EM of bacteriophage phi29 emptied particles treated by low pH without CsCl-gradient-purify 手法: EM (単粒子) / 解像度: 15.0 Å EMDB-6558: Cryo-EM of bacteriophage phi29 emptied particles fusing with liposome after low pH treatment 手法: EM (単粒子) / 解像度: 34.5 Å PDB-5fb4: Crystal structure of the bacteriophage phi29 tail knob protein gp9 truncation variant 手法: X-RAY DIFFRACTION / 解像度: 2.039 Å PDB-5fb5: Crystal structure of the bacteriophage phi29 tail knob protein gp9 手法: X-RAY DIFFRACTION / 解像度: 3.5 Å PDB-5fei: Crystal structure of the bacteriophage phi29 tail knob protein gp9 truncation variant 手法: X-RAY DIFFRACTION / 解像度: 2.604 Å
化合物	ChemComp-PEG: DI(HYDROXYETHYL)ETHER / ジエチレングリコ-ル ChemComp-HOH: WATER
由来	bacillus phage phi29 (ファージ)
キーワード	VIRAL PROTEIN / bacteriophage phi29 / tail knob / tail knob protein gp9 / full-length