View source for 5mup


==Structure of deformed wing virus, a honeybee pathogen==
<SX load='5mup' size='340' side='right' viewer='molstar' caption='[[5mup]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mup]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Deformed_wing_virus Deformed wing virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MUP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mup OCA], [https://pdbe.org/5mup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mup RCSB], [https://www.ebi.ac.uk/pdbsum/5mup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mup ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/L0CTV4_9VIRU L0CTV4_9VIRU] 
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== 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<ref>PMID:28270616</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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[[Category: Deformed wing virus]]
[[Category: Large Structures]]
[[Category: Fuzik T]]
[[Category: Novacek J]]
[[Category: Paxton R]]
[[Category: Plevka P]]
[[Category: Pridal A]]
[[Category: Skubnik K]]