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	Structure of deformed wing virus, a major honey bee pathogen.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 114, Issue 12, Page 3210-3215, Year 2017
Publish date	Mar 21, 2017
Authors	Karel Škubník / Jiří Nováček / Tibor Füzik / Antonín Přidal / Robert J Paxton / Pavel Plevka /
PubMed Abstract	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.
External links	Proc Natl Acad Sci U S A / PubMed:28270616 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.45 - 3.802 Å
Structure data	3570 5mup EMDB-3570, PDB-5mup: Structure of deformed wing virus, a honeybee pathogen Method: EM (single particle) / Resolution: 3.8 Å 3574 5mv5 EMDB-3574, PDB-5mv5: Structure of deformed wing virus, a honeybee pathogen Method: EM (single particle) / Resolution: 3.1 Å 3575 5mv6 EMDB-3575, PDB-5mv6: Structure of deformed wing virus, a honeybee pathogen Method: EM (single particle) / Resolution: 3.5 Å 4009 5l7q EMDB-4009, PDB-5l7q: Structure of deformed wing virus, a honeybee pathogen Method: EM (single particle) / Resolution: 3.5 Å 4014 5l8q EMDB-4014, PDB-5l8q: Structure of deformed wing virus, a honeybee pathogen Method: EM (single particle) / Resolution: 3.5 Å PDB-5g51: High resolution structure of the part of VP3 protein of Deformed Wing Virus forming P-domain Method: X-RAY DIFFRACTION / Resolution: 1.45 Å PDB-5g52: Crystallographic structure of full particle of Deformed Wing Virus Method: X-RAY DIFFRACTION / Resolution: 3.802 Å
Chemicals	ChemComp-HOH: WATER / Water ChemComp-U5P: URIDINE-5'-MONOPHOSPHATE / Uridine monophosphate ChemComp-U: URIDINE-5'-MONOPHOSPHATE / Uridine monophosphate
Source	deformed wing virus apis mellifera (honey bee)
Keywords	VIRAL PROTEIN / PICORNAVIRALES / PICORNAVIRALES IFLAVIRIDAE IFLAVIRUS DWV CAPSID P-DOMAIN JELLYROLL INHIBITOR ANTIVIRAL CATALYTIC SITE PROTEASE LIPASE ESTERASE RECEPTOR / VIRUS / IFLAVIRIDAE / IFLAVIRUS / DWV CAPSID / P JELLYROLL / CATALYTIC SITE PROTEASE / LIPASE ESTERASE RECEPTO / Deformed wing virus / bee pathogen