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| | <StructureSection load='3cab' size='340' side='right'caption='[[3cab]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='3cab' size='340' side='right'caption='[[3cab]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CAB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3CAB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3cab]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CAB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bjh|3bjh]], [[3bfa|3bfa]], [[3bfb|3bfb]], [[3bfh|3bfh]], [[2h8v|2h8v]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3cab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cab OCA], [http://pdbe.org/3cab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cab RCSB], [http://www.ebi.ac.uk/pdbsum/3cab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cab 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=3cab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cab OCA], [https://pdbe.org/3cab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cab RCSB], [https://www.ebi.ac.uk/pdbsum/3cab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cab ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9U9J6_APIME Q9U9J6_APIME] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Apis mellifera]] | | [[Category: Apis mellifera]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bezirard, V]] | + | [[Category: Bezirard V]] |
| - | [[Category: Briand, L]] | + | [[Category: Briand L]] |
| - | [[Category: Cambillau, C]] | + | [[Category: Cambillau C]] |
| - | [[Category: Pernollet, J C]] | + | [[Category: Pernollet JC]] |
| - | [[Category: Pesenti, M E]] | + | [[Category: Pesenti ME]] |
| - | [[Category: Spinelli, S]] | + | [[Category: Spinelli S]] |
| - | [[Category: Tegoni, M]] | + | [[Category: Tegoni M]] |
| - | [[Category: Honeybee]]
| + | |
| - | [[Category: Pheromone binding protein]]
| + | |
| - | [[Category: Pheromone-binding protein]]
| + | |
| - | [[Category: Queen mandibular pheromone]]
| + | |
| - | [[Category: Signal transduction]]
| + | |
| Structural highlights
Function
Q9U9J6_APIME
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The behavior of insects and their perception of their surroundings are driven, in a large part, by odorants and pheromones. This is especially true for social insects, such as the honey bee, where the queen controls the development and the caste status of the other individuals. Pheromone perception is a complex phenomenon relying on a cascade of recognition events, initiated in antennae by pheromone recognition by a pheromone-binding protein and finishing with signal transduction at the axon membrane level. With to the objective of deciphering this initial step, we have determined the structures of the bee antennal pheromone-binding protein (ASP1) in the apo form and in complex with the main component of the queen mandibular pheromonal mixture, 9-keto-2(E)-decenoic acid (9-ODA) and with nonpheromonal components. In the apo protein, the C terminus obstructs the binding site. In contrast, ASP1 complexes have different open conformations, depending on the ligand shape, leading to different volumes of the binding cavity. The binding site integrity depends on the C terminus (111-119) conformation, which involves the interplay of two factors; i.e. the presence of a ligand and a low pH. Ligand binding to ASP1 is favored by low pH, opposite to what is observed with other pheromone-binding proteins, such as those of Bombyx mori and Anopheles gambiae.
Structural basis of the honey bee PBP pheromone and pH-induced conformational change.,Pesenti ME, Spinelli S, Bezirard V, Briand L, Pernollet JC, Tegoni M, Cambillau C J Mol Biol. 2008 Jun 27;380(1):158-69. Epub 2008 Apr 27. PMID:18508083[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pesenti ME, Spinelli S, Bezirard V, Briand L, Pernollet JC, Tegoni M, Cambillau C. Structural basis of the honey bee PBP pheromone and pH-induced conformational change. J Mol Biol. 2008 Jun 27;380(1):158-69. Epub 2008 Apr 27. PMID:18508083 doi:10.1016/j.jmb.2008.04.048
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