1TFJ

Crystal structure of Bovine Glycolipid transfer protein in complex with a fatty acid

Summary for 1TFJ

• Entry DOI: 10.2210/pdb1tfj/pdb
• Descriptor: Glycolipid transfer protein, CHLORIDE ION, DECANOIC ACID, ... (5 entities in total)
• Functional Keywords: glycolipid, lipid transport
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm : P68265
• Total number of polymer chains: 1
• Total formula weight: 25393.81

Authors

Airenne, T.T.,Kidron, H.,West, G.,Nymalm, Y.,Mattjus, P.,Salminen, T.A. (deposition date: 2004-05-27, release date: 2005-08-09, Last modification date: 2024-02-14)

Primary citation

Airenne, T.T.,Kidron, H.,Nymalm, Y.,Nylund, M.,West, G.,Mattjus, P.,Salminen, T.A.
Structural evidence for adaptive ligand binding of glycolipid transfer protein.
J.Mol.Biol., 355:224-236, 2006

PubMed Abstract: 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 angstroms, 1.6 angstroms and 1.8 angstroms resolution, all with a bound fatty acid or glycolipid. The 1.4 angstroms 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.

PubMed: 16309699
DOI: 10.1016/j.jmb.2005.10.031

Experimental method

X-RAY DIFFRACTION (1.61 Å)