3ogn: Difference between revisions
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==Crystal Structure of an Odorant-binding Protein from the Southern House Mosquito Complexed with an Oviposition Pheromone== | |||
<StructureSection load='3ogn' size='340' side='right' caption='[[3ogn]], [[Resolution|resolution]] 1.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ogn]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OGN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CpipJ_CPIJ007604 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7176 Culex quinquefasciatus])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ogn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ogn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ogn RCSB], [http://www.ebi.ac.uk/pdbsum/3ogn PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Odorant binding protein|Odorant binding protein]] | *[[Odorant binding protein|Odorant binding protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Culex quinquefasciatus]] | [[Category: Culex quinquefasciatus]] | ||
[[Category: Clardy, J | [[Category: Clardy, J]] | ||
[[Category: Mao, Y | [[Category: Mao, Y]] | ||
[[Category: Helix bundle]] | [[Category: Helix bundle]] | ||
[[Category: Odorant-binding protein]] | [[Category: Odorant-binding protein]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 11:18, 18 December 2014
Crystal Structure of an Odorant-binding Protein from the Southern House Mosquito Complexed with an Oviposition PheromoneCrystal Structure of an Odorant-binding Protein from the Southern House Mosquito Complexed with an Oviposition Pheromone
Structural highlights
Publication Abstract from PubMedCulex 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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