2fjy
From Proteopedia
(New page: 200px<br /><applet load="2fjy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fjy, resolution 2.300Å" /> '''Crystal Structure o...) |
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| - | [[Image:2fjy.gif|left|200px]]<br /><applet load="2fjy" size=" | + | [[Image:2fjy.gif|left|200px]]<br /><applet load="2fjy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fjy, resolution 2.300Å" /> | caption="2fjy, resolution 2.300Å" /> | ||
'''Crystal Structure of B-form Bombyx mori Pheromone Binding Protein'''<br /> | '''Crystal Structure of B-form Bombyx mori Pheromone Binding Protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The transport of hydrophobic insect pheromones through the aqueous medium | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2FJY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http:// | + | 2FJY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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]. |
==Reference== | ==Reference== | ||
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[[Category: Clardy, J.]] | [[Category: Clardy, J.]] | ||
[[Category: Lautenschlager, C.]] | [[Category: Lautenschlager, C.]] | ||
| - | [[Category: Leal, W | + | [[Category: Leal, W S.]] |
[[Category: alpha helical]] | [[Category: alpha helical]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:12 2008'' |
Revision as of 15:22, 21 February 2008
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Crystal Structure of B-form Bombyx mori Pheromone Binding Protein
Overview
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.
About this Structure
2FJY is a Single protein structure of sequence from Bombyx mori. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 17:22:12 2008
