1gm0: Difference between revisions
New page: left|200px<br /><applet load="1gm0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gm0" /> '''A FORM OF THE PHEROMONE-BINDING PROTEIN FROM... |
No edit summary |
||
| (19 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==A Form of the Pheromone-Binding Protein from Bombyx mori== | ||
Odorants are transmitted by small hydrophobic molecules that cross the | <StructureSection load='1gm0' size='340' side='right'caption='[[1gm0]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1gm0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GM0 FirstGlance]. <br> | |||
</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'>[https://proteopedia.org/fgij/fg.htm?mol=1gm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gm0 OCA], [https://pdbe.org/1gm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gm0 RCSB], [https://www.ebi.ac.uk/pdbsum/1gm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gm0 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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gm/1gm0_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gm0 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Odorants are transmitted by small hydrophobic molecules that cross the aqueous sensillar lymph surrounding the dendrites of the olfactory neurons to stimulate the olfactory receptors. In insects, the transport of pheromones, which are a special class of odorants, is mediated by pheromone-binding proteins (PBPs), which occur at high concentrations in the sensillar lymph. The PBP from the silk moth Bombyx mori (BmPBP) undergoes a pH-dependent conformational transition between the forms BmPBP(A) present at pH 4.5 and BmPBP(B) present at pH 6.5. Here, we describe the NMR structure of BmPBP(A), which consists of a tightly packed arrangement of seven alpha-helices linked by well defined peptide segments and knitted together by three disulfide bridges. A scaffold of four alpha-helices that forms the ligand binding site in the crystal structure of a BmPBP-pheromone complex is preserved in BmPBP(A). The C-terminal dodecapeptide segment, which is in an extended conformation and located on the protein surface in the pheromone complex, forms a regular helix, alpha(7), which is located in the pheromone-binding site in the core of the unliganded BmPBP(A). Because investigations by others indicate that the pH value near the membrane surface is reduced with respect to the bulk sensillar lymph, the pH-dependent conformational transition of BmPBP suggests a novel physiological mechanism of intramolecular regulation of protein function, with the formation of alpha(7) triggering the release of the pheromone from BmPBP to the membrane-standing receptor. | |||
NMR structure reveals intramolecular regulation mechanism for pheromone binding and release.,Horst R, Damberger F, Luginbuhl P, Guntert P, Peng G, Nikonova L, Leal WS, Wuthrich K Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14374-9. Epub 2001 Nov 27. PMID:11724947<ref>PMID:11724947</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1gm0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Odorant binding protein|Odorant binding protein]] | |||
*[[Pheromone binding protein|Pheromone binding protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bombyx mori]] | [[Category: Bombyx mori]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Damberger | [[Category: Damberger F]] | ||
[[Category: Guntert | [[Category: Guntert P]] | ||
[[Category: Horst | [[Category: Horst R]] | ||
[[Category: Leal | [[Category: Leal WS]] | ||
[[Category: Luginbuhl | [[Category: Luginbuhl P]] | ||
[[Category: Nikonova | [[Category: Nikonova L]] | ||
[[Category: Peng | [[Category: Peng G]] | ||
[[Category: Wuthrich | [[Category: Wuthrich K]] | ||
