View source for 2ygu


==Crystal structure of fire ant venom allergen, Sol I 2==
<StructureSection load='2ygu' size='340' side='right'caption='[[2ygu]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ygu]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Solenopsis_invicta Solenopsis invicta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YGU 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HP6:HEPTANE'>HP6</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=2ygu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ygu OCA], [https://pdbe.org/2ygu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ygu RCSB], [https://www.ebi.ac.uk/pdbsum/2ygu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ygu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VA2_SOLIN VA2_SOLIN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sol i 2 is a potent allergen from the venom of red imported fire ant, which contains allergens Sol i 1, Sol i 2, Sol i 3, and Sol i 4 that are known to be powerful triggers of anaphylaxis. Sol i 2 causes IgE antibody production in about one-third of individuals stung by fire ants. Baculovirus recombinant dimeric Sol i 2 was crystallized as a native and selenomethionyl-derivatized protein, and its structure has been determined by single-wavelength anomalous dispersion at 2.6 A resolution. The overall fold of each subunit consists of five helices that enclose a central hydrophobic cavity. The structure is stabilized by three intramolecular disulfide bridges and one intermolecular disulfide bridge. The nearest structural homologue is the sequence-unrelated odorant binding protein and pheromone binding protein LUSH of the fruit fly Drosophila, which may suggest a similar biological function. To test this hypothesis, we measured the reversible binding of various pheromones, plant odorants, and other ligands to Sol i 2 by the changes in N-phenyl-1-naphthylamine fluorescence emission upon binding of ligands that compete with N-phenyl-1-naphthylamine. The highest binding affinity was observed for hydrophobic ligands such as aphid alarm pheromone (E)-beta-farnesene, analogs of ant alarm pheromones, and plant volatiles decane, undecane, and beta-caryophyllene. Conceivably, Sol i 2 may play a role in capturing and/or transporting small hydrophobic ligands such as pheromones, odors, fatty acids, or short-living hydrophobic primers. Molecular surface analysis, in combination with sequence alignment, can explain the serological cross-reactivity observed between some ant species.

Crystal Structure of Sol i 2: A Major Allergen from Fire Ant Venom.,Borer AS, Wassmann P, Schmidt M, Hoffman DR, Zhou JJ, Wright C, Schirmer T, Markovic-Housley Z J Mol Biol. 2011 Nov 12. PMID:22100449<ref>PMID:22100449</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ygu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Solenopsis invicta]]
[[Category: Borer AS]]
[[Category: Markovic-Housley Z]]
[[Category: Schirmer T]]
[[Category: Wassmann P]]