2fjy

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[[Image:2fjy.png|left|200px]]
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==Crystal Structure of B-form Bombyx mori Pheromone Binding Protein==
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<StructureSection load='2fjy' size='340' side='right' caption='[[2fjy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2fjy]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FJY FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7091 Bombyx mori])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fjy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fjy RCSB], [http://www.ebi.ac.uk/pdbsum/2fjy PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/2fjy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_2fjy| PDB=2fjy | SCENE= }}
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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<ref>PMID:16111659</ref>
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===Crystal Structure of B-form Bombyx mori Pheromone Binding Protein===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_16111659}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2fjy]] is a 2 chain structure with sequence from [http://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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:016111659</ref><references group="xtra"/>
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[[Category: Bombyx mori]]
[[Category: Bombyx mori]]
[[Category: Clardy, J.]]
[[Category: Clardy, J.]]

Revision as of 02:12, 30 September 2014

Crystal Structure of B-form Bombyx mori Pheromone Binding Protein

2fjy, resolution 2.30Å

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