2fjy: Difference between revisions
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[[Image:2fjy.gif|left|200px]] | [[Image:2fjy.gif|left|200px]] | ||
'''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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| 2fjy, resolution 2.300Å | |||||||||||||
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| 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
