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 of deformed wing virus, a major honey bee pathogen.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 114, Issue 12, Page 3210-3215, Year 2017
掲載日	2017年3月21日
著者	Karel Škubník / Jiří Nováček / Tibor Füzik / Antonín Přidal / Robert J Paxton / Pavel Plevka /
PubMed 要旨	The worldwide population of western honey bees () is under pressure from habitat loss, environmental stress, and pathogens, particularly viruses that cause lethal epidemics. Deformed wing virus (DWV) ...The worldwide population of western honey bees () is under pressure from habitat loss, environmental stress, and pathogens, particularly viruses that cause lethal epidemics. Deformed wing virus (DWV) from the family , together with its vector, the mite , is likely the major threat to the world's honey bees. However, lack of knowledge of the atomic structures of iflaviruses has hindered the development of effective treatments against them. Here, we present the virion structures of DWV determined to a resolution of 3.1 Å using cryo-electron microscopy and 3.8 Å by X-ray crystallography. The C-terminal extension of capsid protein VP3 folds into a globular protruding (P) domain, exposed on the virion surface. The P domain contains an Asp-His-Ser catalytic triad that is, together with five residues that are spatially close, conserved among iflaviruses. These residues may participate in receptor binding or provide the protease, lipase, or esterase activity required for entry of the virus into a host cell. Furthermore, nucleotides of the DWV RNA genome interact with VP3 subunits. The capsid protein residues involved in the RNA binding are conserved among honey bee iflaviruses, suggesting a putative role of the genome in stabilizing the virion or facilitating capsid assembly. Identifying the RNA-binding and putative catalytic sites within the DWV virion structure enables future analyses of how DWV and other iflaviruses infect insect cells and also opens up possibilities for the development of antiviral treatments.
リンク	Proc Natl Acad Sci U S A / PubMed:28270616 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	1.45 - 3.802 Å
構造データ	3570 5mup EMDB-3570, PDB-5mup: Structure of deformed wing virus, a honeybee pathogen 手法: EM (単粒子) / 解像度: 3.8 Å 3574 5mv5 EMDB-3574, PDB-5mv5: Structure of deformed wing virus, a honeybee pathogen 手法: EM (単粒子) / 解像度: 3.1 Å 3575 5mv6 EMDB-3575, PDB-5mv6: Structure of deformed wing virus, a honeybee pathogen 手法: EM (単粒子) / 解像度: 3.5 Å 4009 5l7q EMDB-4009, PDB-5l7q: Structure of deformed wing virus, a honeybee pathogen 手法: EM (単粒子) / 解像度: 3.5 Å 4014 5l8q EMDB-4014, PDB-5l8q: Structure of deformed wing virus, a honeybee pathogen 手法: EM (単粒子) / 解像度: 3.5 Å PDB-5g51: High resolution structure of the part of VP3 protein of Deformed Wing Virus forming P-domain 手法: X-RAY DIFFRACTION / 解像度: 1.45 Å PDB-5g52: Crystallographic structure of full particle of Deformed Wing Virus 手法: X-RAY DIFFRACTION / 解像度: 3.802 Å
化合物	ChemComp-HOH: WATER / 水 ChemComp-U5P: URIDINE-5'-MONOPHOSPHATE / UMP / ウリジル酸 ChemComp-U: URIDINE-5'-MONOPHOSPHATE / UMP / ウリジル酸
由来	deformed wing virus (ウイルス) apis mellifera (セイヨウミツバチ)
キーワード	VIRAL PROTEIN (ウイルスタンパク質) / PICORNAVIRALES (ピコルナウイルス目) / PICORNAVIRALES IFLAVIRIDAE IFLAVIRUS DWV CAPSID P-DOMAIN JELLYROLL INHIBITOR ANTIVIRAL CATALYTIC SITE PROTEASE LIPASE ESTERASE RECEPTOR / VIRUS (ウイルス) / IFLAVIRIDAE / IFLAVIRUS / DWV CAPSID / P JELLYROLL / CATALYTIC SITE PROTEASE / LIPASE ESTERASE RECEPTO / Deformed wing virus / bee pathogen