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| | ==NMR structure of Antheraea polyphemus pheromone-binding protein 1 at pH 4.5== | | ==NMR structure of Antheraea polyphemus pheromone-binding protein 1 at pH 4.5== |
| - | <StructureSection load='2jpo' size='340' side='right' caption='[[2jpo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2jpo' size='340' side='right'caption='[[2jpo]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jpo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Antpo Antpo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JPO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jpo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Antheraea_polyphemus Antheraea polyphemus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JPO FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gm0|1gm0]], [[1two|1two]], [[1ls8|1ls8]], [[1qwv|1qwv]], [[1xfr|1xfr]], [[1dqe|1dqe]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2jpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jpo OCA], [http://pdbe.org/2jpo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jpo RCSB], [http://www.ebi.ac.uk/pdbsum/2jpo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jpo 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=2jpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jpo OCA], [https://pdbe.org/2jpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jpo RCSB], [https://www.ebi.ac.uk/pdbsum/2jpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jpo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PBP_ANTPO PBP_ANTPO]] This major soluble protein in olfactory sensilla of male moths might serve to solubilize the extremely hydrophobic pheromone molecules and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia. | + | [https://www.uniprot.org/uniprot/PBP_ANTPO PBP_ANTPO] This major soluble protein in olfactory sensilla of male moths might serve to solubilize the extremely hydrophobic pheromone molecules and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jp/2jpo_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jp/2jpo_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Antpo]] | + | [[Category: Antheraea polyphemus]] |
| - | [[Category: Damberger, F F]] | + | [[Category: Large Structures]] |
| - | [[Category: Ishida, Y]] | + | [[Category: Damberger FF]] |
| - | [[Category: Leal, W S]] | + | [[Category: Ishida Y]] |
| - | [[Category: Wuthrich, K]] | + | [[Category: Leal WS]] |
| - | [[Category: Helix insertion]] | + | [[Category: Wuthrich K]] |
| - | [[Category: Insect odorant-binding protein]]
| + | |
| - | [[Category: Ph-dependent conformation]]
| + | |
| - | [[Category: Transport protein]]
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| Structural highlights
Function
PBP_ANTPO This major soluble protein in olfactory sensilla of male moths might serve to solubilize the extremely hydrophobic pheromone molecules and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.
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 NMR structure of the Antheraea polyphemus pheromone-binding protein 1 at pH 4.5, ApolPBP1A, was determined at 20 degrees C. The structure consists of six alpha-helices, which are arranged in a globular fold that encapsulates a central helix alpha7 formed by the C-terminal polypeptide segment 131-142. The 3D arrangement of these helices is anchored by the three disulfide bonds 19-54, 50-108 and 97-117, which were identified by NMR. Superposition of the ApolPBP1A structure with the structure of the homologous pheromone-binding protein of Bombyx mori at pH 4.5, BmorPBPA, yielded an rmsd of 1.7 A calculated for the backbone heavy-atoms N, Calpha and C' of residues 10-142. In contrast, the present ApolPBP1A structure is different from a recently proposed molecular model for a low-pH form of ApolPBP1 that does not contain the central helix alpha7. ApolPBP1 exhibits a pH-dependent transition between two different globular conformations in slow exchange on the NMR chemical shift timescale similar to BmorPBP, suggesting that the two proteins use the same mechanism of ligand binding and ejection. The extensive sequence homology observed for pheromone-binding proteins from moth species further implies that the previously proposed mechanism of ligand ejection involving the insertion of a C-terminal helix into the pheromone-binding site is a general feature of pheromone signaling in moths.
Structural basis of ligand binding and release in insect pheromone-binding proteins: NMR structure of Antheraea polyphemus PBP1 at pH 4.5.,Damberger FF, Ishida Y, Leal WS, Wuthrich K J Mol Biol. 2007 Nov 2;373(4):811-9. Epub 2007 Aug 17. PMID:17884092[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Damberger FF, Ishida Y, Leal WS, Wuthrich K. Structural basis of ligand binding and release in insect pheromone-binding proteins: NMR structure of Antheraea polyphemus PBP1 at pH 4.5. J Mol Biol. 2007 Nov 2;373(4):811-9. Epub 2007 Aug 17. PMID:17884092 doi:10.1016/j.jmb.2007.07.078
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