3ogn: Difference between revisions

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<StructureSection load='3ogn' size='340' side='right'caption='[[3ogn]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='3ogn' size='340' side='right'caption='[[3ogn]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ogn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Culqu Culqu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OGN FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ogn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Culex_quinquefasciatus Culex quinquefasciatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OGN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3OG:(1S)-1-[(2R)-6-OXOTETRAHYDRO-2H-PYRAN-2-YL]UNDECYL+ACETATE'>3OG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CpipJ_CPIJ007604 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7176 CULQU])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3OG:(1S)-1-[(2R)-6-OXOTETRAHYDRO-2H-PYRAN-2-YL]UNDECYL+ACETATE'>3OG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3ogn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ogn OCA], [https://pdbe.org/3ogn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ogn RCSB], [https://www.ebi.ac.uk/pdbsum/3ogn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ogn ProSAT]</span></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=3ogn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ogn OCA], [https://pdbe.org/3ogn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ogn RCSB], [https://www.ebi.ac.uk/pdbsum/3ogn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ogn ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8T6I2_CULQU Q8T6I2_CULQU]
Culex mosquitoes introduce the pathogens responsible for filariasis, West Nile virus, St. Louis encephalitis, and other diseases into humans. Currently, traps baited with oviposition semiochemicals play an important role in detection efforts and could provide an environmentally friendly approach to controlling their populations. The odorant binding proteins (OBPs) in the female's antenna play a crucial, if yet imperfectly understood, role in sensing oviposition cues. Here, we report the X-ray crystallography and NMR 3D structures of OBP1 for Culex quinquefasciatus (CquiOBP1) bound to an oviposition pheromone (5R,6S)-6-acetoxy-5-hexadecanolide (MOP). In both studies, CquiOBP1 had the same overall six-helix structure seen in other insect OBPs, but a detailed analysis revealed an important previously undescribed feature. There are two models for OBP-mediated signal transduction: (i) direct release of the pheromone from an internal binding pocket in a pH-dependent fashion and (ii) detection of a pheromone-induced conformational change in the OBP.pheromone complex. Although CquiOBP1 binds MOP in a pH-dependent fashion, it lacks the C terminus required for the pH-dependent release model. This study shows that CquiOBP binds MOP in an unprecedented fashion using both a small central cavity for the lactone head group and a long hydrophobic channel for its tail.
 
Crystal and solution structures of an odorant-binding protein from the southern house mosquito complexed with an oviposition pheromone.,Mao Y, Xu X, Xu W, Ishida Y, Leal WS, Ames JB, Clardy J Proc Natl Acad Sci U S A. 2010 Oct 18. PMID:20956299<ref>PMID:20956299</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ogn" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Culqu]]
[[Category: Culex quinquefasciatus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Clardy, J]]
[[Category: Clardy J]]
[[Category: Mao, Y]]
[[Category: Mao Y]]
[[Category: Helix bundle]]
[[Category: Odorant-binding protein]]
[[Category: Transport protein]]
Retrieved from "https://proteopedia.org/3ogn"