2fjy
From Proteopedia
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| - | [[Image:2fjy.gif|left|200px]] | + | [[Image:2fjy.gif|left|200px]] |
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| - | '''Crystal Structure of B-form Bombyx mori Pheromone Binding Protein''' | + | {{Structure |
| + | |PDB= 2fjy |SIZE=350|CAPTION= <scene name='initialview01'>2fjy</scene>, resolution 2.300Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= PBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7091 Bombyx mori]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of B-form Bombyx mori Pheromone Binding Protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FJY is a [ | + | 2FJY is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16111659 16111659] |
[[Category: Bombyx mori]] | [[Category: Bombyx mori]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha helical]] | [[Category: alpha helical]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:53:17 2008'' |
Revision as of 14:53, 20 March 2008
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| , resolution 2.300Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | PBP (Bombyx mori) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 16:53:17 2008
