5g52

Crystallographic structure of full particle of Deformed Wing Virus

spinqualitylabelsall models 5g52, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g52 is a 3 chain structure with sequence from Deformed wing virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.802Å Ligands: U5P Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8B3M2_9VIRU Publication Abstract from PubMed The worldwide population of western honey bees (Apis mellifera) is under pressure from habitat loss, environmental stress, and pathogens, particularly viruses that cause lethal epidemics. Deformed wing virus (DWV) from the family Iflaviridae, together with its vector, the mite Varroa destructor, 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 A using cryo-electron microscopy and 3.8 A 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. Structure of deformed wing virus, a major honey bee pathogen.,Skubnik K, Novacek J, Fuzik T, Pridal A, Paxton RJ, Plevka P Proc Natl Acad Sci U S A. 2017 Mar 7. pii: 201615695. doi:, 10.1073/pnas.1615695114. PMID:28270616 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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