3GSH

Three-dimensional structure of a post translational modified barley LTP1

Replaces:  3CEE

Summary for 3GSH

• Entry DOI: 10.2210/pdb3gsh/pdb
• Related: 1MID
• Descriptor: Non-specific lipid-transfer protein 1, ZINC ION, SODIUM ION, ... (6 entities in total)
• Functional Keywords: ltp1, post-transcriptional modification, oxylipin, lipid- binding, lipoprotein, transport, lipid binding protein, disulfide bond, lipid-binding
• Biological source: Hordeum vulgare (barley)
• Total number of polymer chains: 2
• Total formula weight: 20561.47

Authors

Lascombe, M.B.,Prange, T.,Bakan, B.,Marion, D. (deposition date: 2009-03-27, release date: 2009-12-15, Last modification date: 2024-10-30)

Primary citation

Bakan, B.,Hamberg, M.,Larue, V.,Prange, T.,Marion, D.,Lascombe, M.B.
The crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins.
Biochem.Biophys.Res.Commun., 390:780-785, 2009

PubMed Abstract: 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.

PubMed: 19836358
DOI: 10.1016/j.bbrc.2009.10.049

Experimental method

X-RAY DIFFRACTION (1.8 Å)