The crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins.
The barley lipid transfer protein (LTP1) adducted by an alpha-ketol, (9-hydroxy-10-oxo-12(Z)-octadecenoic acid) exhibits an unexpected high lipid transfer activity. The crystal structure of this oxylipin-adducted LTP1, (LTP1b) was determined at 1.8A resolution. The covalently bound oxylipin was partly exposed at the surface of the protein and partly buried within the hydrophobic cavity. The structure of the oxylipidated LTP1 emphasizes the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins when compared to the other members of the family. The plasticity of the hydrophobic cavity and increase of its surface hydrophobicity induced by the oxylipin account for the improvement of the lipid transfer activity of LTP1b. These observations open new perspectives to explore the different biological functions of LTPs, including their allergenic properties.
Bakan
B
B
INRA, Unité de recherches Biopolymères, Interactions, Assemblages, BP71627, La Géraudière, 44316 Nantes cedex 3, France. bakan@nantes.inra.fr
Hamberg
M
M
Larue
V
V
Prangé
T
T
Marion
D
D
Lascombe
M-B
MB
D002352:Carrier Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D050556:Fatty Acid-Binding Proteins; D057927:Hydrophobic and Hydrophilic Interactions; D054883:Oxylipins / Q000737:chemistry*; D011487:Protein Conformation
D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; C422456:Ltp1 protein, barley; D054883:Oxylipins