The crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins
作者： B. Bakan , M. Hamberg , V. Larue , T. Prangé , D. Marion
DOI: 10.1016/J.BBRC.2009.10.049
关键词: Crystal structure 、 Hydrophobicity scales 、 Oxylipin 、 Plant lipid transfer proteins 、 Chemical structure 、 Protein structure 、 Biochemistry 、 Covalent bond 、 Biophysics 、 Chemistry 、 Conjugated system 、 Cell biology 、 Molecular biology
摘要: The barley lipid transfer protein (LTP1) adducted by an alpha-ketol, (9-hydroxy-10-oxo-12(Z)-octadecenoic acid) exhibits unexpected high activity. crystal structure of this oxylipin-adducted LTP1, (LTP1b) was determined at 1.8A resolution. covalently bound oxylipin partly exposed the surface and buried within hydrophobic cavity. oxylipidated LTP1 emphasizes unique plasticity cavity these plant lipid-binding proteins when compared to other members family. increase its hydrophobicity induced account for improvement activity LTP1b. These observations open new perspectives explore different biological functions LTPs, including their allergenic properties.
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