6omw

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<StructureSection load='6omw' size='340' side='right'caption='[[6omw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='6omw' size='340' side='right'caption='[[6omw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6omw]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Aedae Aedae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OMW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OMW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6omw]] is a 9 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=6OMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OMW FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=PAM:PALMITOLEIC+ACID'>PAM</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6og0|6og0]], [[6ogh|6ogh]], [[6oii|6oii]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=PAM:PALMITOLEIC+ACID'>PAM</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5567053, AAEL005772 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7159 AEDAE])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6omw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6omw OCA], [https://pdbe.org/6omw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6omw RCSB], [https://www.ebi.ac.uk/pdbsum/6omw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6omw ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6omw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6omw OCA], [http://pdbe.org/6omw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6omw RCSB], [http://www.ebi.ac.uk/pdbsum/6omw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6omw ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q1HRL7_AEDAE Q1HRL7_AEDAE]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6omw" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aedae]]
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[[Category: Aedes aegypti]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jones, D N]]
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[[Category: Jones DN]]
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[[Category: Wang, J]]
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[[Category: Wang J]]
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[[Category: Chemo-sensory signaling]]
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[[Category: Lipid binding]]
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[[Category: Odorant-binding protein]]
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[[Category: Transport protein]]
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Revision as of 07:07, 3 April 2024

Structure of Aedes aegypti OBP22 in the complex with palmitoleic acid

PDB ID 6omw

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