View source for 6oii


==Structure of Aedes aegypti OBP22 in the complex with arachidonic acid==
<StructureSection load='6oii' size='340' side='right'caption='[[6oii]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6oii]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OII 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACD:ARACHIDONIC+ACID'>ACD</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=6oii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oii OCA], [https://pdbe.org/6oii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oii RCSB], [https://www.ebi.ac.uk/pdbsum/6oii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oii ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OBP22_AEDAE OBP22_AEDAE] Involved in modulation of blood-feeding behavior and capacity in female mosquitoes (PubMed:22479185, PubMed:34634943). Required for normal oviposition (PubMed:34634943). Required for normal fecundity and fertility of female and male mosquitoes (PubMed:34634943). Required for normal expression of VGA1 gene, which encodes the egg yolk protein vitellogenin-A1 (PubMed:34634943). Involved in regulation of spermatozoa development (PubMed:34634943). Required for normal female longevity when mosquitoes are maintained on regular sugar meal (PubMed:34634943). Binds long chain fatty acids (PubMed:32094450).<ref>PMID:22479185</ref> <ref>PMID:32094450</ref> <ref>PMID:34634943</ref>   (Microbial infection) Facilitates shedding of dengue virus type 2 particles into mosquito saliva (PubMed:34634943). Does not affect dengue virus type 2 replication or infection prevalence in midgut and salivary glands at 14 days after blood feeding (PubMed:34634943).<ref>PMID:34634943</ref>   (Microbial infection) Facilitates shedding of Zika virus particles into mosquito saliva (PubMed:34634943). Does not affect Zika virus replication or infection prevalence in midgut and salivary glands at 14 days after blood feeding (PubMed:34634943).<ref>PMID:34634943</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aedes aegypti is the primary vector for transmission of Dengue, Zika and chikungunya viruses. Previously it was shown that Dengue virus infection of the mosquito led to an in increased expression of the odorant binding protein 22 (AeOBP22) within the mosquito salivary gland and that siRNA mediated knockdown of AeOBP22 led to reduced mosquito feeding behaviors. Insect OBPs are implicated in the perception, storage and transport of chemosensory signaling molecules including air-borne odorants and pheromones. AeOBP22 is unusual as it is additionally expressed in multiple tissues, including the antenna, the male reproductive glands and is transferred to females during reproduction, indicating multiple roles in the mosquito life cycle. However, it is unclear what role it plays in these tissues and what ligands it interacts with. Here we present solution and X-ray crystallographic studies that indicate a potential role of AeOBP22 binding to fatty acids, and that the specificity for longer chain fatty acids is regulated by a conformational change in the C-terminal tail that leads to creation of an enlarged binding cavity that enhances binding affinity. This study sheds light onto the native ligands for AeOBP22 and provides insight into its potential functions in different tissues.

Aedes aegypti Odorant Binding Protein 22 selectively binds fatty acids through a conformational change in its C-terminal tail.,Wang J, Murphy EJ, Nix JC, Jones DNM Sci Rep. 2020 Feb 24;10(1):3300. doi: 10.1038/s41598-020-60242-9. PMID:32094450<ref>PMID:32094450</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6oii" style="background-color:#fffaf0;"></div>

==See Also==
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aedes aegypti]]
[[Category: Large Structures]]
[[Category: Jones DN]]
[[Category: Wang J]]