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Tytuł pozycji:

Ligand- and pH-Induced Structural Transition of Gypsy Moth Lymantria dispar Pheromone-Binding Protein 1 (LdisPBP1).

Tytuł:
Ligand- and pH-Induced Structural Transition of Gypsy Moth Lymantria dispar Pheromone-Binding Protein 1 (LdisPBP1).
Autorzy:
Terrado M; Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Okon M; Department of Biochemistry and Molecular Biology, Department of Chemistry, and Michael Smith Laboratories, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada.
McIntosh LP; Department of Biochemistry and Molecular Biology, Department of Chemistry, and Michael Smith Laboratories, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada.
Plettner E; Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Źródło:
Biochemistry [Biochemistry] 2020 Sep 22; Vol. 59 (37), pp. 3411-3426. Date of Electronic Publication: 2020 Sep 11.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Original Publication: Washington, American Chemical Society.
MeSH Terms:
Carrier Proteins/*metabolism
Insect Proteins/*chemistry
Insect Proteins/*metabolism
Pheromones/*metabolism
Animals ; Hydrogen-Ion Concentration ; Ligands ; Moths ; Protein Binding ; Protein Conformation ; Stereoisomerism
Substance Nomenclature:
0 (Carrier Proteins)
0 (Insect Proteins)
0 (Ligands)
0 (Pheromones)
Entry Date(s):
Date Created: 20200903 Date Completed: 20210316 Latest Revision: 20210316
Update Code:
20240104
DOI:
10.1021/acs.biochem.0c00592
PMID:
32877603
Czasopismo naukowe
Pheromone-binding proteins (PBPs) are small, water-soluble proteins found in the lymph of pheromone-sensing hairs. PBPs are essential in modulating pheromone partitioning in the lymph and at pheromone receptors of olfactory sensory neurons. The function of a PBP is associated with its ability to structurally convert between two conformations. Although mechanistic details remain unclear, it has been proposed that the structural transition between these forms is affected by two factors: pH and the presence or absence of ligand. To better understand the PBP conformational transition, the structure of the gypsy moth ( Lymantria dispar ) LdisPBP1 was elucidated at pH 4.5 and 35 °C using nuclear magnetic resonance spectroscopy. In addition, the effects of sample pH and binding of the species' pheromone, (+)-disparlure, (7 R ,8 S )-epoxy-2-methyloctadecane, and its enantiomer were monitored via 15 N HSQC spectroscopy. LdisPBP1 in acidic conditions has seven helices, with its C-terminal residues forming the seventh helix within the pheromone-binding pocket and its N-terminal residues disordered. Under conditions where this conformation is made favorable, free LdisPBP1 would have limited ligand binding capacity due to the seventh helix occupying the internal binding pocket. Our findings suggest that even in the presence of 4-fold ligand at acidic pH, LdisPBP1 is only ∼60% in its pheromone-bound form. Furthermore, evidence of a different LdisPBP1 form is seen at higher pH, with the transition pH between 5.6 and 6.0. This suggests that LdisPBP1 at neutral pH exists as a mixture of at least two conformations. These findings have implications concerning the PBP ligand binding and release mechanism.

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