3GSH: Three-dimensional structure of a post translational modified barley LTP1

Citation:
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.
PDB ID: 3GSHDownload
MMDB ID: 78733
PDB Deposition Date: 2009/3/27
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3GSH: monomeric; determined by author and by software (PISA)
Molecular Components in 3GSH
Label Count Molecule
Protein (1 molecule)
1
Non-specific Lipid-transfer Protein 1(Gene symbol: ltp1)
Molecule annotation
Chemicals (7 molecules)
1
2
2
2
3
1
4
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.