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	Structural atlas of a human gut crassvirus.
ジャーナル・号・ページ	Nature, Vol. 617, Issue 7960, Page 409-416, Year 2023
掲載日	2023年5月3日
著者	Oliver W Bayfield / Andrey N Shkoporov / Natalya Yutin / Ekaterina V Khokhlova / Jake L R Smith / Dorothy E D P Hawkins / Eugene V Koonin / Colin Hill / Alfred A Antson /
PubMed 要旨	CrAssphage and related viruses of the order Crassvirales (hereafter referred to as crassviruses) were originally discovered by cross-assembly of metagenomic sequences. They are the most abundant ...CrAssphage and related viruses of the order Crassvirales (hereafter referred to as crassviruses) were originally discovered by cross-assembly of metagenomic sequences. They are the most abundant viruses in the human gut, are found in the majority of individual gut viromes, and account for up to 95% of the viral sequences in some individuals. Crassviruses are likely to have major roles in shaping the composition and functionality of the human microbiome, but the structures and roles of most of the virally encoded proteins are unknown, with only generic predictions resulting from bioinformatic analyses. Here we present a cryo-electron microscopy reconstruction of Bacteroides intestinalis virus ΦcrAss001, providing the structural basis for the functional assignment of most of its virion proteins. The muzzle protein forms an assembly about 1 MDa in size at the end of the tail and exhibits a previously unknown fold that we designate the 'crass fold', that is likely to serve as a gatekeeper that controls the ejection of cargos. In addition to packing the approximately 103 kb of virus DNA, the ΦcrAss001 virion has extensive storage space for virally encoded cargo proteins in the capsid and, unusually, within the tail. One of the cargo proteins is present in both the capsid and the tail, suggesting a general mechanism for protein ejection, which involves partial unfolding of proteins during their extrusion through the tail. These findings provide a structural basis for understanding the mechanisms of assembly and infection of these highly abundant crassviruses.
リンク	Nature / PubMed:37138077 / PubMed Central
手法	EM (単粒子)
解像度	3.01 - 4.4 Å
構造データ	14088 7qof EMDB-14088, PDB-7qof: Icosahedral capsid of the phicrAss001 virion 手法: EM (単粒子) / 解像度: 3.01 Å 14089 7qog EMDB-14089, PDB-7qog: Portal protein assembly of the phicrAss001 virion with C12 symmetry imposed 手法: EM (単粒子) / 解像度: 3.09 Å 14090 7qoh EMDB-14090, PDB-7qoh: Unique vertex of the phicrAss001 virion with C5 symmetry imposed 手法: EM (単粒子) / 解像度: 3.32 Å 14091 7qoi EMDB-14091, PDB-7qoi: Unique vertex of the phicrAss001 virion 手法: EM (単粒子) / 解像度: 3.62 Å 14092 7qoj EMDB-14092, PDB-7qoj: Tail barrel assembly of the phicrAss001 virion with C12 symmetry imposed 手法: EM (単粒子) / 解像度: 3.21 Å 14093 7qok EMDB-14093: Tip section. PDB-7qok: Tail muzzle assembly of the phicrAss001 virion with C6 symmetry imposed 手法: EM (単粒子) / 解像度: 3.38 Å 14094 7qol EMDB-14094, PDB-7qol: Tail assembly of the phicrAss001 virion with C6 symmetry imposed 手法: EM (単粒子) / 解像度: 3.33 Å EMDB-14100: Asymmetric reconstruction of the phicrAss001 virion 手法: EM (単粒子) / 解像度: 4.4 Å
化合物	ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-HOH: WATER
由来	bacteroides phage crass001 (ファージ)
キーワード	VIRUS / crAssphage / bacteriophage / DNA virus / portal / connector / vertex / capsid / tail / muzzle / ring