View source for 5g51


==High resolution structure of the part of VP3 protein of Deformed Wing Virus forming P-domain==
<StructureSection load='5g51' size='340' side='right'caption='[[5g51]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5g51]] is a 1 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=5G51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G51 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</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=5g51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g51 OCA], [https://pdbe.org/5g51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g51 RCSB], [https://www.ebi.ac.uk/pdbsum/5g51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g51 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8B3M2_9VIRU Q8B3M2_9VIRU] 
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 5g51" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[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]]