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	Structure and Function of Hoc-A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages.
ジャーナル・号・ページ	Viruses, Vol. 15, Issue 7, Year 2023
掲載日	2023年7月7日
著者	Andrei Fokine / Mohammad Zahidul Islam / Qianglin Fang / Zhenguo Chen / Lei Sun / Venigalla B Rao /
PubMed 要旨	Bacteriophage T4 is decorated with 155 180 Å-long fibers of the highly antigenic outer capsid protein (Hoc). In this study, we describe a near-atomic structural model of Hoc by combining cryo- ...Bacteriophage T4 is decorated with 155 180 Å-long fibers of the highly antigenic outer capsid protein (Hoc). In this study, we describe a near-atomic structural model of Hoc by combining cryo-electron microscopy and AlphaFold structure predictions. It consists of a conserved C-terminal capsid-binding domain attached to a string of three variable immunoglobulin (Ig)-like domains, an architecture well-preserved in hundreds of Hoc molecules found in phage genomes. Each T4-Hoc fiber attaches randomly to the center of gp23* hexameric capsomers in one of the six possible orientations, though at the vertex-proximal hexamers that deviate from 6-fold symmetry, Hoc binds in two preferred orientations related by 180° rotation. Remarkably, each Hoc fiber binds to all six subunits of the capsomer, though the interactions are greatest with three of the subunits, resulting in the off-centered attachment of the C-domain. Biochemical analyses suggest that the acidic Hoc fiber (pI, ~4-5) allows for the clustering of virions in acidic pH and dispersion in neutral/alkaline pH. Hoc appears to have evolved as a sensing device that allows the phage to navigate its movements through reversible clustering-dispersion transitions so that it reaches its destination, the host bacterium, and persists in various ecological niches such as the human/mammalian gut.
リンク	Viruses / PubMed:37515203 / PubMed Central
手法	EM (単粒子)
解像度	3.3 - 3.4 Å
構造データ	PDB-8t1x: T4 highly immunogenic outer capsid protein C-terminal domain bound to *the vertex-proximal gp23 capsomer of the isometric head in two preferred orientations 手法: ELECTRON MICROSCOPY / 解像度: 3.3 Å PDB-8t9r: T4 highly immunogenic outer capsid protein C-terminal domain bound to a vertex-proximal gp23* capsomer of the prolate capsid in two preferred orientations. 手法: ELECTRON MICROSCOPY / 解像度**: 3.4 Å
由来	escherichia phage t4 (ファージ)
キーワード	VIRAL PROTEIN (ウイルスタンパク質) / bacteriophage (ファージ) / capsid (カプシド) / T4 head / Hoc / highly immunogenic outer capsid protein / virus decoration protein / immunoglobulin-like domains / antigen display / vaccine (ワクチン)