View source for 6qq4


==Odorant-binding protein dmelOBP28a from Drosophila melanogaster==
<StructureSection load='6qq4' size='340' side='right'caption='[[6qq4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qq4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QQ4 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]] 1.998&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</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=6qq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qq4 OCA], [https://pdbe.org/6qq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qq4 RCSB], [https://www.ebi.ac.uk/pdbsum/6qq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qq4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OB28A_DROME OB28A_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Odorant-binding proteins (OBPs) are small soluble proteins that are thought to transport hydrophobic odorants across the aqueous sensillar lymph to olfactory receptors. A recent study revealed that OBP28a, one of the most abundant Drosophila OBPs, is not required for odorant transport, but acts in buffering rapid odour variation in the odorant environment. To further unravel and decipher its functional role, we expressed recombinant OBP28a and characterized its binding specificity. Using a fluorescent binding assay, we found that OBP28a binds a restricted number of floral-like chemicals, including ss-ionone, with an affinity in the micromolar range. We solved the X-ray crystal structure of OBP28a, which showed extensive conformation changes upon ligand binding. Mutant flies genetically deleted for the OBP28a gene showed altered responses to ss-ionone at a given concentration range, supporting its essential role in the detection of specific compounds present in the natural environment of the fly.

The Drosophila odorant-binding protein 28a is involved in the detection of the floral odour ss-ionone.,Gonzalez D, Rihani K, Neiers F, Poirier N, Fraichard S, Gotthard G, Chertemps T, Maibeche M, Ferveur JF, Briand L Cell Mol Life Sci. 2020 Jul;77(13):2565-2577. doi: 10.1007/s00018-019-03300-4., Epub 2019 Sep 28. PMID:31564000<ref>PMID:31564000</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qq4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Briand L]]
[[Category: Gonzalez D]]
[[Category: Gotthard G]]
[[Category: Neiers F]]