Structural Evidence for Adaptive Ligand Binding of Glycolipid Transfer Protein

Glycolipids participate in many important cellular processes and they are bound and transferred with high specificity by glycolipid transfer protein (GLTP). We have solved three different X-ray structures of bovine GLTP at 1.4 Å, 1.6 Å and 1.8 Å resolution, all with a bound fatty acid or glycolipid....

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Bibliographic Details
Published in:Journal of molecular biology 2006-01, Vol.355 (2), p.224-236
Main Authors: Airenne, Tomi T., Kidron, Heidi, Nymalm, Yvonne, Nylund, Matts, West, Gun, Mattjus, Peter, Salminen, Tiina A.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Cattle
cavity
conformational change
crystal structure
Crystallography, X-Ray
Disulfides - chemistry
fluorescence
Glycolipids - metabolism
homology modeling
Ligands
Molecular Sequence Data
Sequence Alignment
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Summary:Glycolipids participate in many important cellular processes and they are bound and transferred with high specificity by glycolipid transfer protein (GLTP). We have solved three different X-ray structures of bovine GLTP at 1.4 Å, 1.6 Å and 1.8 Å resolution, all with a bound fatty acid or glycolipid. The 1.4 Å structure resembles the recently characterized apo-form of the human GLTP but the other two structures represent an intermediate conformation of the apo-GLTPs and the human lactosylceramide-bound GLTP structure. These novel structures give insight into the mechanism of lipid binding and how GLTP may conformationally adapt to different lipids. Furthermore, based on the structural comparison of the GLTP structures and the three-dimensional models of the related Podospora anserina HET-C2 and Arabidopsis thaliana accelerated cell death protein, ACD11, we give structural explanations for their specific lipid binding properties.
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2005.10.031