Pheromone binding protein: Difference between revisions

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<StructureSection load='3bfa' size='340' side='right' caption='Pheromone binding protein of honey bee complex with pheromone (PDB code [[3bfa]]).' scene=''>
__TOC__
==Introduction==
==Introduction==
<StructureSection load='3bfa' size='340' side='right' caption='Pheromone binding protein of ''Apis mellifera'' scene=''>
'''Pheromone binding proteins''' [http://en.wikipedia.org/wiki/Pheromone_binding_protein (PBP)] are type of Odorant binding proteins [http://en.wikipedia.org/wiki/Odorant-binding_protein (OBP)] - soluble proteins mediating the early stages of volatiles detection in both insects and vertebrates<ref>DOI:10.3389/fphys.2014.00320</ref>. The volatiles (pheromones and other small hydrophobic molecules) are solubilized by the OBPs and activate the chemoreceptors.  
Pheromone binding proteins are soluble proteins invovled in the early stages of pheromone detection.
As a model protein of this family we will further describe the well investigated Pheromone binding protein of the honey bee.


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As a model protein of this family we will further describe the well investigated Pheromone binding protein of the honey bee, ASP1.


Pheromone-binding protein [http://www.uniprot.org/uniprot/Q9U9J6/ ASP] of the honeybee [http://en.wikipedia.org/wiki/Apis_mellifera ''Apis mellifera''] L. (Hymenoptera: Apidea) was first isolated and charecterised by Danty et al. (1998)<ref>DOI:10.1016/j.jmb.2008.04.048</ref> from the bee antennae.
== Pheromone-binding protein ASP1 ==


or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
Chemical communication is crucial in social insects, where a complicated and delicate system of signals must be maintained in order to preserve the fragile equilibrium between the queen and the workers. In the hive of the honey bee [http://en.wikipedia.org/wiki/Apis_mellifera ''Apis mellifera''] this equilibrium exists partially due to the extraction of blend of substances called queen mandibular pheromone [http://en.wikipedia.org/wiki/Honey_bee_pheromones#Queen_mandibular_pheromone (QMP)], by the queen <ref>Winston, M.L., 1987. The Biology of the Honey Bee. Harvard University Press, Cambridge, MA.</ref>. The three major component of the QMP blend are: 9-keto-2(E)-decenoic acid (9-ODA) and 9-hydroxy-2(E)-decenoic acid (9-HDA R-(−) or S-(+)).   
Pheromone-binding protein [http://www.uniprot.org/uniprot/Q9U9J6/ ASP1] of the honeybee [http://en.wikipedia.org/wiki/Apis_mellifera ''Apis mellifera''] L. (Hymenoptera: Apidea) was first isolated and characterized by Danty ''et al''. (1998)<ref>DOI:10.1016/j.jmb.2008.04.048</ref> from the bee antennae.  


== Structure ==
== Structure ==
[[3bfa]] 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=3BFA OCA].
The protein is composed of 144 amino acids, which forms 6 alpha helices. Three <scene name='60/609542/Disulfide_bonds/1'>3 disulfide bonds</scene> formed by 6 Cystein residues tied four helices: disulfide 20–51 between H1 and H3, 47– 98 between H3 and H6, and 107–89 between H6 and H5.


== Function ==
== Interaction with the ligand 9-ODA==
One of the main components of the QMP <scene name='60/609542/9-oda/3'>9-ODA</scene>, is binding to the protein binding site along with a <scene name='60/609542/Glycerol/2'>glycerol molecule</scene>.The carboxyl end of 9-ODA points towards the solvent, and has no bonds with residues of the protein. The residues in the binding site are <scene name='60/609542/Binding_site/3'>hydrophobic</scene>, and the connection between 9-ODA and ASP1 involve hydrogen bonds.


== Disease ==
</StructureSection>
 
==3D structures of pheromone-binding protein==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
 
* Pheromone binding protein


== Relevance ==
**[[2h8v]], [[3bjh]], [[3cab]], [[3cdn]], [[3cz2]] – bPBP residues 26-144 – honey bee<br />
**[[3d73]], [[3d74]], [[3d75]], [[3d76]], [[3d77]], [[3d78]] - bPBP residues 26-144 (mutant)<br />
**[[1dqe]], [[2fjy]] – sPBP – silkworm<br />
**[[1xfr]] – sPBP – NMR<br />
**[[1gm0]] – sPBP (mutant) – NMR<br />
**[[1qwv]], [[1two]], [[2jpo]], [[6um9]] – mPBP – moth - NMR<br />
**[[6vq5]] – mPBP <br />
**[[7uo6]] – PBP2 – corn borer - NMR<br />
**[[7vw8]], [[7vw9]] – bwPBP1 - bollworm<br />


== Structural highlights ==
* Pheromone binding protein complex


This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
**[[3bfa]], [[3bfb]], [[3bfh]], [[3cyz]] – bPBP residues 26-144 + pheromone<br />
**[[3cz0]], [[3cz1]] - bPBP residues 26-144 + N-butyl benzene sulfonamide<br />
**[[3fe6]], [[3fe8]], [[3fe9]] - bPBP residues 26-144 + methyldotetracontane<br />
**[[2p70]] – sPBP + odorant<br />
**[[2p71]] – sPBP + iodohexadecane<br />
**[[4inw]], [[4inx]] – PBP + hexadecadienal – ''Amyelois transitella''<br />
**[[7vwa]] – bwPBP1 + odorant <br />
}}


</StructureSection>
== References ==
== References ==
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<references/>
[[Category: Topic Page]]

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Nurit Eliash, Michal Harel