2fjy

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of B-form Bombyx mori Pheromone Binding Protein

Structural highlights

2fjy is a 2 chain structure with sequence from Bombyx mori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PBP_BOMMO This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol 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 transport of hydrophobic insect pheromones through the aqueous medium surrounding their receptors is assisted by pheromone-binding proteins (PBPs). The protein from the silkworm moth Bombyx mori, BmorPBP, exhibits a pH-dependent conformational change postulated to trigger the release of the pheromone bombykol to its receptor. At low pH, an alpha-helix occupies the same binding pocket that houses the pheromone in the BmorPBP-bombykol complex at high pH. We have determined the crystal structure of apo BmorPBP at a resolution of 2.3 angstroms and pH 7.5, which has surprisingly a structure similar to the A-form. These data suggest that BmorPBP undergoes a ligand-dependent conformational change in addition to the previously described pH-dependent conformational change. Analysis of the alpha-helix occupying the binding pocket reveals an amphipathic helix with three acidic residues along one face that are conserved among lepidopteran PBPs and may be involved in a conformational transition of BmorPBP at the receptor membrane.

Coil-to-helix transition and ligand release of Bombyx mori pheromone-binding protein.,Lautenschlager C, Leal WS, Clardy J Biochem Biophys Res Commun. 2005 Oct 7;335(4):1044-50. PMID:16111659^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lautenschlager C, Leal WS, Clardy J. Coil-to-helix transition and ligand release of Bombyx mori pheromone-binding protein. Biochem Biophys Res Commun. 2005 Oct 7;335(4):1044-50. PMID:16111659 doi:10.1016/j.bbrc.2005.07.176

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fjy"

Categories: Bombyx mori | Large Structures | Clardy J | Lautenschlager C | Leal WS

@@ Line 3: / Line 3: @@
 <StructureSection load='2fjy' size='340' side='right'caption='[[2fjy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2fjy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bommo Bommo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FJY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2fjy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FJY FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PBP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7091 BOMMO])</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]] 2.3&#8491;</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=2fjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fjy OCA], [https://pdbe.org/2fjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fjy RCSB], [https://www.ebi.ac.uk/pdbsum/2fjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fjy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PBP_BOMMO PBP_BOMMO]] This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.
+[https://www.uniprot.org/uniprot/PBP_BOMMO PBP_BOMMO] This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/2fjy_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>
   </jmolCheckbox>
@@ Line 35: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Bommo]]
+[[Category: Bombyx mori]]
 [[Category: Large Structures]]
-[[Category: Clardy, J]]
+[[Category: Clardy J]]
-[[Category: Lautenschlager, C]]
+[[Category: Lautenschlager C]]
-[[Category: Leal, W S]]
+[[Category: Leal WS]]
-[[Category: Alpha helical]]
-[[Category: Transport protein]]

2fjy

From Proteopedia

Current revision

Crystal Structure of B-form Bombyx mori Pheromone Binding Protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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