3bfh: Difference between revisions
New page: '''Unreleased structure''' The entry 3bfh is ON HOLD until Paper Publication Authors: Pesenti, M.E., Spinelli, S., Bezirard, V., Briand, L., Pernollet, J.C., Tegoni, M., Cambillau, C. ... |
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{{STRUCTURE_3bfh| PDB=3bfh | SCENE= }} | |||
'''Crystal structure of a pheromone binding protein from Apis mellifera in complex with hexadecanoic acid''' | |||
==Overview== | |||
The behavior of insects and their perception of their surroundings are driven, in a large part, by odorants and pheromones. This is especially true for social insects, such as the honey bee, where the queen controls the development and the caste status of the other individuals. Pheromone perception is a complex phenomenon relying on a cascade of recognition events, initiated in antennae by pheromone recognition by a pheromone-binding protein and finishing with signal transduction at the axon membrane level. With to the objective of deciphering this initial step, we have determined the structures of the bee antennal pheromone-binding protein (ASP1) in the apo form and in complex with the main component of the queen mandibular pheromonal mixture, 9-keto-2(E)-decenoic acid (9-ODA) and with nonpheromonal components. In the apo protein, the C terminus obstructs the binding site. In contrast, ASP1 complexes have different open conformations, depending on the ligand shape, leading to different volumes of the binding cavity. The binding site integrity depends on the C terminus (111-119) conformation, which involves the interplay of two factors; i.e. the presence of a ligand and a low pH. Ligand binding to ASP1 is favored by low pH, opposite to what is observed with other pheromone-binding proteins, such as those of Bombyx mori and Anopheles gambiae. | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 | ==About this Structure== | ||
3BFH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BFH OCA]. | |||
==Reference== | |||
Structural Basis of the Honey Bee PBP Pheromone and pH-induced Conformational Change., Pesenti ME, Spinelli S, Bezirard V, Briand L, Pernollet JC, Tegoni M, Cambillau C, J Mol Biol. 2008 Apr 27;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18508083 18508083] | |||
[[Category: Apis mellifera]] | |||
[[Category: Single protein]] | |||
[[Category: Bezirard, V.]] | |||
[[Category: Briand, L.]] | |||
[[Category: Cambillau, C.]] | |||
[[Category: Pernollet, J C.]] | |||
[[Category: Pesenti, M E.]] | |||
[[Category: Spinelli, S.]] | |||
[[Category: Tegoni, M.]] | |||
[[Category: Apis mellifera]] | |||
[[Category: Hexadecanoic acid]] | |||
[[Category: Honeybee]] | |||
[[Category: Pheromone binding protein]] | |||
[[Category: Pheromone-binding protein]] | |||
[[Category: Queen mandibular pheromone]] | |||
[[Category: Signal transduction]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:47:02 2008'' | |||
Revision as of 10:47, 11 June 2008
Crystal structure of a pheromone binding protein from Apis mellifera in complex with hexadecanoic acid
OverviewOverview
The behavior of insects and their perception of their surroundings are driven, in a large part, by odorants and pheromones. This is especially true for social insects, such as the honey bee, where the queen controls the development and the caste status of the other individuals. Pheromone perception is a complex phenomenon relying on a cascade of recognition events, initiated in antennae by pheromone recognition by a pheromone-binding protein and finishing with signal transduction at the axon membrane level. With to the objective of deciphering this initial step, we have determined the structures of the bee antennal pheromone-binding protein (ASP1) in the apo form and in complex with the main component of the queen mandibular pheromonal mixture, 9-keto-2(E)-decenoic acid (9-ODA) and with nonpheromonal components. In the apo protein, the C terminus obstructs the binding site. In contrast, ASP1 complexes have different open conformations, depending on the ligand shape, leading to different volumes of the binding cavity. The binding site integrity depends on the C terminus (111-119) conformation, which involves the interplay of two factors; i.e. the presence of a ligand and a low pH. Ligand binding to ASP1 is favored by low pH, opposite to what is observed with other pheromone-binding proteins, such as those of Bombyx mori and Anopheles gambiae.
About this StructureAbout this Structure
3BFH is a Single protein structure of sequence from Apis mellifera. Full crystallographic information is available from OCA.
ReferenceReference
Structural Basis of the Honey Bee PBP Pheromone and pH-induced Conformational Change., Pesenti ME, Spinelli S, Bezirard V, Briand L, Pernollet JC, Tegoni M, Cambillau C, J Mol Biol. 2008 Apr 27;. PMID:18508083 Page seeded by OCA on Wed Jun 11 10:47:02 2008